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Title: Atomic Resolution Modeling of the Ferredoxin:[FeFe] Hydrogenase Complex from Chlamydomonas reinhardtii

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 H2 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 ferredoxin:hydrogenase 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 ferredoxin:HydA2 interaction is energetically favored over the alternative candidate by 20kcal/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 H2 evolution, and suggests potential mutagenic strategies to modulate electron flow to HydA2.

Authors:
; ; ;
Publication Date:
Research Org.:
National Renewable Energy Lab. (NREL), Golden, CO (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
981976
DOE Contract Number:  
AC36-08GO28308
Resource Type:
Journal Article
Journal Name:
Biophysical Journal
Additional Journal Information:
Journal Volume: 93; Journal Issue: November 2007; Journal ID: ISSN 0006-3495
Country of Publication:
United States
Language:
English
Subject:
08 HYDROGEN; 09 BIOMASS FUELS; 59 BASIC BIOLOGICAL SCIENCES; 71 CLASSICAL AND QUANTUM MECHANICS, GENERAL PHYSICS; BIOLOGICAL PATHWAYS; CHLAMYDOMONAS; COMPLEXES; ELECTRON TRANSFER; ELECTRONS; EVOLUTION; FERREDOXIN; FREE ENERGY; HYDROGENASES; INTERACTIONS; LICENSES; POTENTIALS; PROTEINS; PROTONS; REDUCTION; RESOLUTION; SIMULATION; WATER; Computational Sciences

Citation Formats

Chang, C H, King, P W, Ghirardi, M L, and Kim, K. Atomic Resolution Modeling of the Ferredoxin:[FeFe] Hydrogenase Complex from Chlamydomonas reinhardtii. United States: N. p., 2007. Web. doi:10.1529/biophysj.107.108589.
Chang, C H, King, P W, Ghirardi, M L, & Kim, K. Atomic Resolution Modeling of the Ferredoxin:[FeFe] Hydrogenase Complex from Chlamydomonas reinhardtii. United States. https://doi.org/10.1529/biophysj.107.108589
Chang, C H, King, P W, Ghirardi, M L, and Kim, K. 2007. "Atomic Resolution Modeling of the Ferredoxin:[FeFe] Hydrogenase Complex from Chlamydomonas reinhardtii". United States. https://doi.org/10.1529/biophysj.107.108589.
@article{osti_981976,
title = {Atomic Resolution Modeling of the Ferredoxin:[FeFe] Hydrogenase Complex from Chlamydomonas reinhardtii},
author = {Chang, C H and King, P W and Ghirardi, M L and Kim, K},
abstractNote = {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 H2 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 ferredoxin:hydrogenase 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 ferredoxin:HydA2 interaction is energetically favored over the alternative candidate by 20kcal/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 H2 evolution, and suggests potential mutagenic strategies to modulate electron flow to HydA2.},
doi = {10.1529/biophysj.107.108589},
url = {https://www.osti.gov/biblio/981976}, journal = {Biophysical Journal},
issn = {0006-3495},
number = November 2007,
volume = 93,
place = {United States},
year = {Thu Nov 01 00:00:00 EDT 2007},
month = {Thu Nov 01 00:00:00 EDT 2007}
}