Atomic resolution modeling of the ferredoxin:[FeFe] hydrogenase complex from Chlamydomonas reinhardtii.
Biophys J
; 93(9): 3034-45, 2007 Nov 01.
Article
em En
| MEDLINE
| ID: mdl-17660315
ABSTRACT
The [FeFe] hydrogenases HydA1 and HydA2 in the green alga Chlamydomonas reinhardtii catalyze the final reaction in a remarkable metabolic pathway allowing this photosynthetic organism to produce H(2) from water in the chloroplast. A [2Fe-2S] ferredoxin is a critical branch point in electron flow from Photosystem I toward a variety of metabolic fates, including proton reduction by hydrogenases. To better understand the binding determinants involved in ferredoxinhydrogenase interactions, we have modeled Chlamydomonas PetF1 and HydA2 based on amino-acid sequence homology, and produced two promising electron-transfer model complexes by computational docking. To characterize these models, quantitative free energy calculations at atomic resolution were carried out, and detailed analysis of the interprotein interactions undertaken. The protein complex model we propose for ferredoxinHydA2 interaction is energetically favored over the alternative candidate by 20 kcal/mol. This proposed model of the electron-transfer complex between PetF1 and HydA2 permits a more detailed view of the molecular events leading up to H(2) evolution, and suggests potential mutagenic strategies to modulate electron flow to HydA2.
Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Modelos Moleculares
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Chlamydomonas reinhardtii
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Proteínas de Algas
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Ferredoxinas
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Hidrogenase
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Ferro
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Proteínas Ferro-Enxofre
Limite:
Animals
Idioma:
En
Revista:
Biophys J
Ano de publicação:
2007
Tipo de documento:
Article
País de afiliação:
Estados Unidos