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1.
Prikl Biokhim Mikrobiol ; 39(5): 571-6, 2003.
Article in Russian | MEDLINE | ID: mdl-14593872

ABSTRACT

Incubation of cells of the cyanobacterium Spirulina platensis under conditions of exposure to low-intensity (2-3 microE m-2 s-1) red light, which was predominantly absorbed by photosystem I (PS I), caused atypical adaptation changes. Invariable pigment composition and stoichiometry of photosystems was observed in the cells incubated under these conditions against the background of a decrease in the rate of photosynthetic fixation of CO2 (by one-half) and a 1.5-fold increase in the rate of dark respiration relative to cells incubated under conditions of exposure to green light. Comparison of these data with a high rate of dark relaxation of P700+ in the presence of diuron suggests that deficiency of reduced equivalents at the donor side of PS I in the Spirulina cells exposed to red light is compensated by electron supply from the respiratory chain NAD(P)H dehydrogenase complex.


Subject(s)
Cyanobacteria/physiology , Light , Adaptation, Physiological , Carbon Dioxide/metabolism , Chlorophyll/metabolism , Cyanobacteria/metabolism , FMN Reductase/metabolism , Lighting , Oxidation-Reduction , Photosynthesis , Pigments, Biological/biosynthesis
2.
Bioelectrochemistry ; 53(1): 61-71, 2001 Jan.
Article in English | MEDLINE | ID: mdl-11206926

ABSTRACT

Cadmium and lead metals deposited on CdS particles are shown to act as substrates--electron donors for enzymes, hydrogenase from Thiocapsa roseopersicina (HG), NAD-dependent hydrogenase from Alcaligenes eutrophus (NLH), and ferredoxin:NADP oxidoreductase (FNR) from Chlorella in the formation of hydrogen, NADH and NADPH, respectively. Adsorption of the enzyme on the surface of the metallized CdS particle is required for enzymatic oxidation of metal. The maximum rates for the formation of hydrogen and NADH catalyzed by hydrogenase and NAD-dependent hydrogenase with metals as electron donors are comparable with the rates obtained for these enzymes using soluble substrates. Kinetic analysis of the enzymatic oxidation of cadmium metal has revealed that the rate decreases mainly due to the formation of a solid product, which is supposed to be Cd(OH)2. The deceleration of lead oxidation catalyzed by hydrogenase proceeds at the expense of the inhibitory effect of the formed Pb2+. The enzymatic oxidation of electrochemically prepared cadmium metal is also shown. Based on these results, a new mechanism of action of the enzymes involved in anaerobic biocorrosion is proposed. By this mechanism, the enzyme accelerates the process of metal dissolution through a mediatorless catalysis of the reduction of the enzyme substrate.


Subject(s)
Cadmium Compounds/chemistry , Cadmium/chemistry , Lead/chemistry , Oxidoreductases/metabolism , Sulfides/chemistry , Algal Proteins/chemistry , Algal Proteins/metabolism , Bacterial Proteins/chemistry , Bacterial Proteins/metabolism , Electrochemistry/methods , Enzymes, Immobilized/chemistry , Enzymes, Immobilized/metabolism , Ferredoxin-NADP Reductase/chemistry , Ferredoxin-NADP Reductase/metabolism , Hydrogenase/chemistry , Hydrogenase/metabolism , Kinetics , Models, Chemical , NADH, NADPH Oxidoreductases/chemistry , NADH, NADPH Oxidoreductases/metabolism , Oxidation-Reduction , Oxidoreductases/chemistry , Photochemistry
3.
Biokhimiia ; 45(10): 1755-60, 1980 Oct.
Article in Russian | MEDLINE | ID: mdl-6263359

ABSTRACT

The light electron transport in non-photosynthetic mutants of Chlamydomonas reinhardii A-36 and A-68 with a decreased content of cytochrome c553 was studied. The light-induced changes of absorption at 520, 559, 563 nm were shown to occur in the films of intact cells and in cell fragments. However, no maximum of the "light minus dark" difference absorption spectra of mutants belonging to cytochrome c553 was revealed. The electron transport from water to NADP+ or ferricyanide in the mutants was completely blocked; however, it was partly restored by an addition of exogenous cytochrome c553 to the cell fragments. A conclusion on the genetic damage of cytochrome c553 in mutants A-36 and A-68 was made. The localization of the cytochrome in the electron transport chain between the photosystems was demonstrated.


Subject(s)
Chlamydomonas/metabolism , Cytochrome c Group/metabolism , Chlamydomonas/genetics , Cytochrome c Group/genetics , Electron Transport , Kinetics , Light , Mutation , NADP/metabolism , Photosynthesis , Spectrophotometry
4.
Biokhimiia ; 44(11): 2005-12, 1979 Nov.
Article in Russian | MEDLINE | ID: mdl-546443

ABSTRACT

The photo-dependent absorption changes of cytochrome f in bean chloroplasts and native leaves treated with the polyene antibiotics surgumycin and filipin were studied. Upon incubation of the chloroplasts or leaves with the antibiotics the value of the photo-induced signal of cytochrome f decreased considerably; however, the kinetics of the cytochrome oxidation under the effect of the exciting light and dark reduction remained unchanged. An addition of plastocyanin to the suspension of the antibiotic-treated chloroplasts, which contained no artificial donors and acceptors, only slightly increased the absolute value of the photo-induced signal of cytochrome f. An addition of plastocyanin to the chloroplasts containing the dichlorophenolindophenol-ascorbate-methylviologen system, sharply changed the kinetics of the cytochrome f photoconversions. A simultaneous registration of the photo-induced signal of cytochrome f and the photochemical activity of photosystem I of the antibiotic-treated chloroplasts revealed differences in the degree of inhibition of the photosystem I activity and decrease of the absolute value of the cytochrome f signal. The data obtained are discussed in terms of possible alternative pathways of electron transfer in the part of the electron transporting chain under study.


Subject(s)
Anti-Bacterial Agents/pharmacology , Chloroplasts/metabolism , Cytochromes/metabolism , Filipin/pharmacology , Polyenes/pharmacology , Chloroplasts/drug effects , Electron Transport , Kinetics , Light , Plants , Spectrophotometry
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