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1.
Science ; 373(6557): 871-876, 2021 08 20.
Artigo em Inglês | MEDLINE | ID: mdl-34282049

RESUMO

DeepMind presented notably accurate predictions at the recent 14th Critical Assessment of Structure Prediction (CASP14) conference. We explored network architectures that incorporate related ideas and obtained the best performance with a three-track network in which information at the one-dimensional (1D) sequence level, the 2D distance map level, and the 3D coordinate level is successively transformed and integrated. The three-track network produces structure predictions with accuracies approaching those of DeepMind in CASP14, enables the rapid solution of challenging x-ray crystallography and cryo-electron microscopy structure modeling problems, and provides insights into the functions of proteins of currently unknown structure. The network also enables rapid generation of accurate protein-protein complex models from sequence information alone, short-circuiting traditional approaches that require modeling of individual subunits followed by docking. We make the method available to the scientific community to speed biological research.


Assuntos
Aprendizado Profundo , Conformação Proteica , Dobramento de Proteína , Proteínas/química , Proteínas ADAM/química , Sequência de Aminoácidos , Simulação por Computador , Microscopia Crioeletrônica , Cristalografia por Raios X , Bases de Dados de Proteínas , Proteínas de Membrana/química , Modelos Moleculares , Complexos Multiproteicos/química , Redes Neurais de Computação , Subunidades Proteicas/química , Proteínas/fisiologia , Receptores Acoplados a Proteínas G/química , Esfingosina N-Aciltransferase/química
2.
Org Biomol Chem ; 19(2): 439-445, 2021 01 21.
Artigo em Inglês | MEDLINE | ID: mdl-33331366

RESUMO

Biocatalysts are receiving increased attention in the field of selective oxyfunctionalization of C-H bonds, with cytochrome P450 monooxygenases (CYP450s), and the related peroxygenases, leading the field. Here we report on the substrate promiscuity of CYP505A30, previously characterized as a fatty acid hydroxylase. In addition to its regioselective oxyfunctionalization of saturated fatty acids (ω-1 - ω-3 hydroxylation), primary fatty alcohols are also accepted with similar regioselectivities. Moreover, alkanes such as n-octane and n-decane are also readily accepted, allowing for the production of non-vicinal diols through sequential oxygenation.

3.
Angew Chem Int Ed Engl ; 60(11): 5644-5665, 2021 03 08.
Artigo em Inglês | MEDLINE | ID: mdl-32330347

RESUMO

Reductions play a key role in organic synthesis, producing chiral products with new functionalities. Enzymes can catalyse such reactions with exquisite stereo-, regio- and chemoselectivity, leading the way to alternative shorter classical synthetic routes towards not only high-added-value compounds but also bulk chemicals. In this review we describe the synthetic state-of-the-art and potential of enzymes that catalyse reductions, ranging from carbonyl, enone and aromatic reductions to reductive aminations.


Assuntos
Aminas/metabolismo , Oxirredutases/metabolismo , Aminas/química , Biocatálise , Estrutura Molecular , Oxirredução , Oxirredutases/química , Estereoisomerismo
4.
Sci Rep ; 9(1): 20088, 2019 12 27.
Artigo em Inglês | MEDLINE | ID: mdl-31882753

RESUMO

Cytochrome P450 reductases (CPRs) are diflavin oxidoreductases that supply electrons to type II cytochrome P450 monooxygenases (CYPs). In addition, it can also reduce other proteins and molecules, including cytochrome c, ferricyanide, and different drugs. Although various CPRs have been functionally and structurally characterized, the overall mechanism and its interaction with different redox acceptors remain elusive. One of the main problems regarding electron transfer between CPRs and CYPs is the so-called "uncoupling", whereby NAD(P)H derived electrons are lost due to the reduced intermediates' (FAD and FMN of CPR) interaction with molecular oxygen. Additionally, the decay of the iron-oxygen complex of the CYP can also contribute to loss of reducing equivalents during an unproductive reaction cycle. This phenomenon generates reactive oxygen species (ROS), leading to an inefficient reaction. Here, we present the study of the CPR from Candida tropicalis (CtCPR) lacking the hydrophobic N-terminal part (Δ2-22). The enzyme supports the reduction of cytochrome c and ferricyanide, with an estimated 30% uncoupling during the reactions with cytochrome c. The ROS produced was not influenced by different physicochemical conditions (ionic strength, pH, temperature). The X-ray structures of the enzyme were solved with and without its cofactor, NADPH. Both CtCPR structures exhibited the closed conformation. Comparison with the different solved structures revealed an intricate ionic network responsible for the regulation of the open/closed movement of CtCPR.


Assuntos
Candida tropicalis/enzimologia , NADPH-Ferri-Hemoproteína Redutase/metabolismo , Cristalografia por Raios X , Transporte de Elétrons , NADPH-Ferri-Hemoproteína Redutase/química , Oxirredução , Conformação Proteica
5.
Nat Commun ; 10(1): 4178, 2019 09 13.
Artigo em Inglês | MEDLINE | ID: mdl-31519878

RESUMO

Continuous low-level supply or in situ generation of hydrogen peroxide (H2O2) is essential for the stability of unspecific peroxygenases, which are deemed ideal biocatalysts for the selective activation of C-H bonds. To envisage potential large scale applications of combined catalytic systems the reactions need to be simple, efficient and produce minimal by-products. We show that gold-palladium nanoparticles supported on TiO2 or carbon have sufficient activity at ambient temperature and pressure to generate H2O2 from H2 and O2 and supply the oxidant to the engineered unspecific heme-thiolate peroxygenase PaDa-I. This tandem catalyst combination facilitates efficient oxidation of a range of C-H bonds to hydroxylated products in one reaction vessel with only water as a by-product under conditions that could be easily scaled.

6.
Org Lett ; 21(17): 7024-7027, 2019 09 06.
Artigo em Inglês | MEDLINE | ID: mdl-31423791

RESUMO

A novel biosynthetic pathway for the production of natural 2-phenylethanol from cinnamaldehyde is reported. An ene-reductase (OYE)-mediated selective hydrogenation of cinnamaldehyde to hydrocinnamaldehyde is followed by a regioselective Baeyer-Villiger oxidation (BVMO) to produce the corresponding formate ester that either spontaneously hydrolyzes to 2-phenylethanol in water or is assisted by a formate dehydrogenase (FDH). This cascade reaction is performed in a one-pot fashion at ambient temperature and pressure. High selectivity and complete conversion were achieved.


Assuntos
Acroleína/análogos & derivados , Oxirredutases/metabolismo , Álcool Feniletílico/metabolismo , Acroleína/química , Acroleína/metabolismo , Estrutura Molecular , Álcool Feniletílico/química , Pressão , Temperatura
7.
Nat Prod Rep ; 36(2): 326-353, 2019 02 20.
Artigo em Inglês | MEDLINE | ID: mdl-30074603

RESUMO

Covering: up to end of June 2018 Baeyer-Villiger monooxygenases (BVMOs) are flavin-dependent enzymes that catalyse the oxidation of ketones and cyclic ketones to esters and lactones, respectively, by using molecular oxygen and NAD(P)H. BVMOs also catalyse sulfoxidations and N-oxidations. BVMOs are widely studied as attractive biocatalysts, but also catalyse key reactions in metabolic pathways of the organisms from which they are sourced. BVMOs are involved in the primary metabolism of atypical carbon sources, thereby conferring an evolutionary advantage to the host organism. In addition, BVMOs catalyse a plethora of diverse Baeyer-Villiger and heteroatom oxidations in the construction of complex secondary metabolites. These natural products often have attractive biological properties, such as anti-bacterial, anti-cancer and anti-proliferative activity, and can have clinical applications. In contrast, BVMOs are also involved in the synthesis of microbial toxins. This review will discuss the inherent roles of type I, type II and type O BVMOs in the metabolism of microorganisms.


Assuntos
Bactérias/metabolismo , Produtos Biológicos/metabolismo , Oxigenases de Função Mista/química , Oxigenases de Função Mista/metabolismo , Micotoxinas/metabolismo , Álcoois/química , Álcoois/metabolismo , Alcanos/metabolismo , Antibacterianos/química , Antibacterianos/metabolismo , Dinitrocresóis/metabolismo , Fungos/metabolismo , Cetonas/metabolismo , Oxirredução , Metabolismo Secundário , Xenobióticos/metabolismo
8.
Chembiochem ; 20(1): 96-102, 2019 01 02.
Artigo em Inglês | MEDLINE | ID: mdl-30252998

RESUMO

Biocatalytic production of lactones, and in particular ϵ-caprolactone (CL), have gained increasing interest as a greener route to polymer building blocks, especially through the use of Baeyer-Villiger monooxygenases (BVMOs). Despite several advances in the field, BVMOs, however, still suffer several practical limitations. Alcohol dehydrogenase (ADH)-mediated lactonization of diols in turn has received far less attention and very few enzymes have been identified for the conversion of diols to lactones, with horse-liver ADH (HLADH) remaining the catalyst of choice. Screening of a diverse panel of ADHs, AaSDR-1, a member of the short-chain dehydrogenase/reductase family, was found to produce ϵ-caprolactone from hexane-1,6-diol. Moreover, cofactor regeneration by an NADH oxidase eliminated the requirement of co-substrates, yielding water as the sole by-product. Despite lower turnover frequencies as compared to HLADH, higher selectivity was found for the production of CL, with HLADH forming significant amounts of 6-hydroxyhexanoic acid and adipic acid through aldehyde dehydrogenation/oxidation of the gem-diol intermediates. Also, CL yield were shown to be dependent on buffer choice, as structural elucidation of a Tris adduct confirmed the buffer amine to react with aliphatic aldehydes forming a Schiff-base intermediate which through further ADH oxidation, forms a tricyclic acetal product.


Assuntos
Glicóis/química , Redutases-Desidrogenases de Cadeia Curta/química , Animais , Bactérias/enzimologia , Biocatálise , Caproatos/metabolismo , Ciclização , Fungos/enzimologia , Lactonas/metabolismo , Modelos Químicos , Oxirredução , Plantas/enzimologia , Especificidade por Substrato , Trometamina/química
9.
Toxins (Basel) ; 10(12)2018 12 05.
Artigo em Inglês | MEDLINE | ID: mdl-30563144

RESUMO

Aflatoxins are carcinogenic mycotoxins that are produced by the filamentous fungus Aspergillus flavus, a contaminant of numerous food crops. Aflatoxins are synthesised via the aflatoxin biosynthesis pathway, with the enzymes involved encoded by the aflatoxin biosynthesis gene cluster. MoxY is a type I Baeyer⁻Villiger monooxygenase (BVMO), responsible for the conversion of hydroxyversicolorone (HVN) and versicolorone (VN) to versiconal hemiacetal acetate (VHA) and versiconol acetate (VOAc), respectively. Using mRNA data, an intron near the C-terminus was identified that is alternatively spliced, creating two possible MoxY isoforms which exist in vivo, while analysis of the genomic DNA suggests an alternative start codon leading to possible elongation of the N-terminus. These four variants of the moxY gene were recombinantly expressed in Escherichia coli, and their activity evaluated with respect to their natural substrates HVN and VN, as well as surrogate ketone substrates. Activity of the enzyme is absolutely dependent on the additional 22 amino acid residues at the N-terminus. Two MoxY isoforms with alternative C-termini, MoxYAltN and MoxYAltNC, converted HVN and VN, in addition to a range of ketone substrates. Stability and flavin-binding data suggest that MoxYAltN is, most likely, the dominant isoform. MoxYAltNC is generated by intron splicing, in contrast to intron retention, which is the most prevalent type of alternative splicing in ascomycetes. The alternative C-termini did not alter the substrate acceptance profile, or regio- or enantioselectivity of the enzyme, but did significantly affect the solubility and stability.


Assuntos
Proteínas Fúngicas/genética , Oxigenases/genética , Aflatoxinas/metabolismo , Processamento Alternativo , Antraquinonas/metabolismo , Aspergillus flavus/enzimologia , Aspergillus flavus/genética , Escherichia coli/enzimologia , Escherichia coli/genética , Proteínas Fúngicas/metabolismo , Isoenzimas/genética , Isoenzimas/metabolismo , Oxigenases/metabolismo
10.
Chem Asian J ; 13(23): 3601-3610, 2018 Dec 04.
Artigo em Inglês | MEDLINE | ID: mdl-30256534

RESUMO

Cyclic esters and amides (lactones and lactams) are important active ingredients and polymer building blocks. In recent years, numerous biocatalytic methods for their preparation have been developed including enzymatic and chemoenzymatic Baeyer-Villiger oxidations, oxidative lactonisation of diols, and reductive lactonisation and lactamisation of ketoesters. The current state of the art of these methods is reviewed.


Assuntos
Lactamas/síntese química , Lactonas/síntese química , Biocatálise , Técnicas de Química Sintética/métodos , Hidrolases/química , Lactamas/química , Lactonas/química , Oxigenases de Função Mista/química , Oxirredução
11.
Proteins ; 85(12): 2252-2257, 2017 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-28833623

RESUMO

Ene-reductases (ERs), or Old Yellow Enzymes, catalyze the asymmetric reduction of various activated alkenes. This class of biocatalysts is considered an attractive alternative to current chemical technologies for hydrogenation due to their high selectivity and specificity. Here the X-ray crystal structure of RmER, a "thermophilic"-like ER from Ralstonia (Cupriavidus) metallidurans, is reported. Unlike other members of this class of ERs, RmER is monomeric in solution which we previously related to its atypical elongated C-terminus. A typical dimer interface was however observed in our crystal structure, with the conserved Arg-"finger" forming part of the adjacent monomer's active site and the elongated C-terminus extending into the active site through contacting the "capping" domain. This dimerization also resulted in the loss of one FMN cofactor from each dimer pair. This potential transient dimerization and dissociation of FMN could conceivably explain the rapid rates previously observed when an FMN light-driven cofactor regeneration system was used during catalysis with RmER.


Assuntos
Proteínas de Bactérias/química , NADPH Desidrogenase/química , Ralstonia/química , Sequência de Aminoácidos , Proteínas de Bactérias/genética , Proteínas de Bactérias/metabolismo , Sítios de Ligação , Biocatálise , Clonagem Molecular , Cristalografia por Raios X , Escherichia coli/genética , Escherichia coli/metabolismo , Mononucleotídeo de Flavina/química , Mononucleotídeo de Flavina/metabolismo , Flavina-Adenina Dinucleotídeo/química , Flavina-Adenina Dinucleotídeo/metabolismo , Expressão Gênica , Modelos Moleculares , NADPH Desidrogenase/genética , NADPH Desidrogenase/metabolismo , Oxirredução , Plasmídeos/química , Plasmídeos/metabolismo , Ligação Proteica , Conformação Proteica em alfa-Hélice , Conformação Proteica em Folha beta , Domínios e Motivos de Interação entre Proteínas , Multimerização Proteica , Ralstonia/enzimologia , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo , Alinhamento de Sequência , Homologia de Sequência de Aminoácidos , Especificidade por Substrato
12.
Eng Life Sci ; 17(1): 71-76, 2017 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-32624730

RESUMO

Old yellow enzymes are able to catalyze asymmetric C=C reductions. A mediated electroenzymatic process to regenerate the NADPH in combination with an old yellow enzyme was investigated. Due to the fact that the overall process was affected by a broad set of parameters, a design of experiments (DoE) approach was chosen to identify suitable process conditions. Process conditions with high productivities of up to 2.27 mM/h in combination with approximately 90% electron transfer efficiency were identified.

13.
Chem Commun (Camb) ; 50(87): 13180-200, 2014 Nov 11.
Artigo em Inglês | MEDLINE | ID: mdl-24902635

RESUMO

The scope and limitations of oxygenases as catalysts for preparative organic synthesis is discussed.


Assuntos
Biocatálise , Oxigênio/metabolismo , Oxigenases/metabolismo , Estrutura Molecular , Oxigênio/química , Oxigenases/química
14.
ACS Synth Biol ; 2(2): 83-92, 2013 Feb 15.
Artigo em Inglês | MEDLINE | ID: mdl-23656371

RESUMO

Saturation mutagenesis probes define sections of the vast protein sequence space. However, even if randomization is limited this way, the combinatorial numbers problem is severe. Because diversity is created at the codon level, codon redundancy is a crucial factor determining the necessary effort for library screening. Additionally, due to the probabilistic nature of the sampling process, oversampling is required to ensure library completeness as well as a high probability to encounter all unique variants. Our trick employs a special mixture of three primers, creating a degeneracy of 22 unique codons coding for the 20 canonical amino acids. Therefore, codon redundancy and subsequent screening effort is significantly reduced, and a balanced distribution of codon per amino acid is achieved, as demonstrated exemplarily for a library of cyclohexanone monooxygenase. We show that this strategy is suitable for any saturation mutagenesis methodology to generate less-redundant libraries.


Assuntos
Códon , Mutagênese Insercional/métodos , Proteínas/genética , Aminoácidos/genética , Técnicas de Química Combinatória/métodos , Primers do DNA/genética , Biblioteca Gênica , Código Genético , Oxigenases/genética
15.
Org Lett ; 15(1): 180-3, 2013 Jan 04.
Artigo em Inglês | MEDLINE | ID: mdl-23256747

RESUMO

A series of synthetic nicotinamide cofactors were synthesized to replace natural nicotinamide cofactors and promote enoate reductase (ER) catalyzed reactions without compromising the activity or stereoselectivity of the bioreduction process. Conversions and enantioselectivities of >99% were obtained for C═C bioreductions, and the process was successfully upscaled. Furthermore, high chemoselectivity was observed when employing these nicotinamide cofactor mimics (mNADs) with crude extracts in ER-catalyzed reactions.


Assuntos
Niacinamida/síntese química , Oxirredutases atuantes sobre Doadores de Grupo CH-CH/metabolismo , Catálise , Técnicas de Química Combinatória , Mimetismo Molecular , Estrutura Molecular , NAD/química , NAD/metabolismo , Niacinamida/química , Oxirredutases atuantes sobre Doadores de Grupo CH-CH/química
16.
Chem Commun (Camb) ; 48(53): 6630-2, 2012 Jul 07.
Artigo em Inglês | MEDLINE | ID: mdl-22555193

RESUMO

A bi-enzymatic cascade for the redox-isomerisation of allylic alcohol is presented. Coupling of an alcohol dehydrogenase to an enoate reductase has been successfully applied in one pot for the isomerisation of an allylic alcohol to the corresponding ketone. Critical parameters for yield and selectivity have been investigated.


Assuntos
Biocatálise , Modelos Biológicos , Álcool Desidrogenase/química , Concentração de Íons de Hidrogênio , Isomerismo , Oxirredução , Propanóis/química
17.
Appl Microbiol Biotechnol ; 96(6): 1507-16, 2012 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-22410745

RESUMO

CYP153A6 is a well-studied terminal alkane hydroxylase which has previously been expressed in Pseudomonas putida and Escherichia coli by using the pCom8 plasmid. In this study, CYP153A6 was successfully expressed in E. coli BL21(DE3) by cloning the complete operon from Mycobacterium sp. HXN-1500, also encoding the ferredoxin reductase and ferredoxin, into pET28b(+). LB medium with IPTG as well as auto-induction medium was used to express the proteins under the T7 promoter. A maximum concentration of 1.85 µM of active CYP153A6 was obtained when using auto-induction medium, while with IPTG induction of LB cultures, the P450 concentration peaked at 0.6-0.8 µM. Since more biomass was produced in auto-induction medium, the specific P450 content was often almost the same, 0.5-1.0 µmol P450 g (DCW)⁻¹, for both methods. Analytical scale whole-cell biotransformations of n-octane were conducted with resting cells, and it was found that high P450 content in biomass did not necessarily result in high octanol production. Whole cells from LB cultures induced with IPTG gave higher specific and volumetric octanol formation rates than biomass from auto-induction medium. A maximum of 8.7 g octanol L (BRM)⁻¹ was obtained within 24 h (0.34 g L (BRM)⁻¹ h⁻¹) with IPTG-induced cells containing only 0.20 µmol P450 g (DCW)⁻¹, when glucose (22 g L (BRM)⁻¹) was added for cofactor regeneration.


Assuntos
Proteínas de Bactérias/genética , Citocromo P-450 CYP4A/genética , Escherichia coli/metabolismo , Mycobacterium/enzimologia , Octanos/metabolismo , Óperon , Proteínas de Bactérias/metabolismo , Citocromo P-450 CYP4A/metabolismo , Escherichia coli/genética , Expressão Gênica , Hidroxilação , Mycobacterium/genética
18.
Chembiochem ; 11(18): 2589-96, 2010 Dec 10.
Artigo em Inglês | MEDLINE | ID: mdl-21080396

RESUMO

Baeyer-Villiger monooxygenases (BVMOs) catalyze the conversion of ketones and cyclic ketones into esters and lactones, respectively. Cyclohexanone monooxygenase (CHMO) from Acinetobacter sp. NCIMB 9871 is known to show an impressive substrate scope as well as exquisite chemo-, regio-, and enantioselectivity in many cases. Large-scale synthetic applications of CHMO are hampered, however, by the instability of the enzyme. Oxidation of cysteine and methionine residues contributes to this instability. Designed mutations of all the methionine and cysteine residues in the CHMO wild type (WT) showed that the amino acids labile towards oxidation are mostly either surface-exposed or located within the active site, whereas the two methionine residues identified for thermostabilization are buried within the folded protein. Combinatorial mutations gave rise to two stabilized mutants with either oxidative or thermal stability, without compromising the activity or stereoselectivity of the enzyme. The most oxidatively stabilized mutant retained nearly 40 % of its activity after incubation with H(2)O(2) (0.2 M), whereas the wild-type enzyme's activity was completely abolished at concentrations as low as 5 mM H(2)O(2). We propose that oxidation-stable mutants might well be a "prerequisite" for thermostabilization, because laboratory-evolved thermostability in CHMO might be masked by a high degree of oxidation instability.


Assuntos
Acinetobacter/enzimologia , Mutação , Oxigenases/genética , Oxigenases/metabolismo , Engenharia de Proteínas , Acinetobacter/genética , Estabilidade Enzimática , Peróxido de Hidrogênio/metabolismo , Modelos Moleculares , Oxirredução , Oxigenases/química , Engenharia de Proteínas/métodos , Especificidade por Substrato , Temperatura
19.
Biochem Biophys Res Commun ; 393(3): 426-31, 2010 Mar 12.
Artigo em Inglês | MEDLINE | ID: mdl-20138824

RESUMO

Recent characterization of the chromate reductase (CrS) from the thermophile Thermus scotoductus SA-01 revealed this enzyme to be related to the Old Yellow Enzyme (OYE) family. Here, we report the structure of a thermostable OYE homolog in its holoform at 2.2A as well as its complex with p-hydroxybenzaldehyde (pHBA). The enzyme crystallized as octamers with the monomers showing a classical TIM barrel fold which upon dimerization yields the biologically active form of the protein. A sulfate ion is bound above the si-side of the non-covalently bound FMN cofactor in the oxidized solved structure but is displaced upon pHBA binding. The active-site architecture is highly conserved as with other members of this enzyme family. The pHBA in the CrS complex is positioned by hydrogen bonding to the two conserved catalytic-site histidines. The most prominent structural difference between CrS and other OYE homologs is the size of the "capping domain". Thermostabilization of the enzyme is achieved in part through increased proline content within loops and turns as well as increased intersubunit interactions through hydrogen bonding and complex salt bridge networks. CrS is able to reduce the C=C bonds of alpha,beta-unsaturated carbonyl compounds with a preference towards cyclic substrates however no activity was observed towards beta-substituted substrates. Mutational studies have confirmed the role of Tyr177 as the proposed proton donor although reduction could still occur at a reduced rate when this residue was mutated to phenylalanine.


Assuntos
NADPH Desidrogenase/química , Thermus/enzimologia , Domínio Catalítico , Cristalografia por Raios X , Estabilidade Enzimática , Temperatura Alta , Estrutura Secundária de Proteína
20.
Biotechnol Lett ; 31(6): 845-9, 2009 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-19229481

RESUMO

Dissimilatory reduction of vanadium(V) by Enterobacter cloacae EV-SA01, isolated from a gold mine at 1.6 km below surface, is shown to occur anaerobically as well as aerobically. Growth rates were unaffected by up to 2 mM V(2)O(5). Reduction of vanadium(V) was growth phase-dependent and resulted in cell deformities and precipitation of the vanadium in its lower oxidation states. The vanadate reductase activity was membrane-associated and coupled the oxidation of NADH to the reduction of vanadate.


Assuntos
Enterobacter cloacae/metabolismo , Microbiologia do Solo , Vanádio/metabolismo , Aerobiose , Anaerobiose , Membrana Celular/enzimologia , Enterobacter cloacae/citologia , Enterobacter cloacae/crescimento & desenvolvimento , Enterobacter cloacae/isolamento & purificação , NAD/metabolismo , Oxirredução , África do Sul
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