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TitleStructural insight on the mechanism of an electron-bifurcating [FeFe] hydrogenase.
Journal, issue, pagesElife, Vol. 11, Year 2022
Publish dateAug 26, 2022
AuthorsChris Furlan / Nipa Chongdar / Pooja Gupta / Wolfgang Lubitz / Hideaki Ogata / James N Blaza / James A Birrell /
PubMed AbstractElectron bifurcation is a fundamental energy conservation mechanism in nature in which two electrons from an intermediate-potential electron donor are split so that one is sent along a high-potential ...Electron bifurcation is a fundamental energy conservation mechanism in nature in which two electrons from an intermediate-potential electron donor are split so that one is sent along a high-potential pathway to a high-potential acceptor and the other is sent along a low-potential pathway to a low-potential acceptor. This process allows endergonic reactions to be driven by exergonic ones and is an alternative, less recognized, mechanism of energy coupling to the well-known chemiosmotic principle. The electron-bifurcating [FeFe] hydrogenase from (HydABC) requires both NADH and ferredoxin to reduce protons generating hydrogen. The mechanism of electron bifurcation in HydABC remains enigmatic in spite of intense research efforts over the last few years. Structural information may provide the basis for a better understanding of spectroscopic and functional information. Here, we present a 2.3 Å electron cryo-microscopy structure of HydABC. The structure shows a heterododecamer composed of two independent 'halves' each made of two strongly interacting HydABC heterotrimers connected via a [4Fe-4S] cluster. A central electron transfer pathway connects the active sites for NADH oxidation and for proton reduction. We identified two conformations of a flexible iron-sulfur cluster domain: a 'closed bridge' and an 'open bridge' conformation, where a Zn site may act as a 'hinge' allowing domain movement. Based on these structural revelations, we propose a possible mechanism of electron bifurcation in HydABC where the flavin mononucleotide serves a dual role as both the electron bifurcation center and as the NAD reduction/NADH oxidation site.
External linksElife / PubMed:36018003 / PubMed Central
MethodsEM (single particle)
Resolution2.3 - 2.8 Å
Structure data

13199

7p5h

EMDB-13199, PDB-7p5h:
TmHydABC- D2 map
Method: EM (single particle) / Resolution: 2.3 Å

13254

7p8n

EMDB-13254, PDB-7p8n:
TmHydABC- T. maritima hydrogenase with bridge closed
Method: EM (single particle) / Resolution: 2.8 Å

13257

7p91

EMDB-13257, PDB-7p91:
TmHydABC- T. maritima bifurcating hydrogenase with bridge domain closed
Method: EM (single particle) / Resolution: 2.8 Å

13258

7p92

EMDB-13258, PDB-7p92:
TmHydABC- T. maritima bifurcating hydrogenase with bridge domain up
Method: EM (single particle) / Resolution: 2.7 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE / Flavin mononucleotide

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER / Water

Source
  • Thermotoga maritima MSB8 (bacteria)
  • thermotoga maritima (strain atcc 43589 / dsm 3109 / jcm 10099 / nbrc 100826 / msb8) (bacteria)
KeywordsOXIDOREDUCTASE / Hydrogenase / bifurcation / confurcaction / cryoEM / electron transfer / complex

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