Redox Intermediates of Desulfovibrio gigas [NiFe] Hydrogenase Generated Under Hydrogen

Teixeira, Miguel; Moura, Isabel; Xavier, António V.; Moura, José J. G.; LeGall, Jean; Dervartanian, D.V.; Peck, Harry D.; Huynh, Boi Hanh

doi:10.1016/s0021-9258(19)84725-7

Cited by 168 publications

(132 citation statements)

References 63 publications

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“…Examples include the haem chain in the aforementioned photosynthetic reaction centre of Rps. viridis [92], the FeS cluster chain in mitochondrial complex I [88,98] and the FeS cluster chain in the NiFe hydrogenase of Desulfovibrio gigas [99]. (These are macroscopic potentials, though; the electrostatic interactions between cofactors can exacerbate the differences in macroscopic midpoint potentials, which would mean smaller differences for 4Fe [51] 2Fe [75] 4Fe [75] [91].…”

Section: Redox Potentialsmentioning

confidence: 99%

Multi-haem cytochromes inShewanella oneidensisMR-1: structures, functions and opportunities

Breuer

Rosso

Blumberger

et al. 2015

J. R. Soc. Interface.

224

186

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Multi-haem cytochromes are employed by a range of microorganisms to transport electrons over distances of up to tens of nanometres. Perhaps the most spectacular utilization of these proteins is in the reduction of extracellular solid substrates, including electrodes and insoluble mineral oxides of Fe(III) and Mn(III/IV), by species of Shewanella and Geobacter. However, multihaem cytochromes are found in numerous and phylogenetically diverse prokaryotes where they participate in electron transfer and redox catalysis that contributes to biogeochemical cycling of N, S and Fe on the global scale. These properties of multi-haem cytochromes have attracted much interest and contributed to advances in bioenergy applications and bioremediation of contaminated soils. Looking forward, there are opportunities to engage multi-haem cytochromes for biological photovoltaic cells, microbial electrosynthesis and developing bespoke molecular devices. As a consequence, it is timely to review our present understanding of these proteins and we do this here with a focus on the multitude of functionally diverse multi-haem cytochromes in Shewanella oneidensis MR-1. We draw on findings from experimental and computational approaches which ideally complement each other in the study of these systems: computational methods can interpret experimentally determined properties in terms of molecular structure to cast light on the relation between structure and function. We show how this synergy has contributed to our understanding of multi-haem cytochromes and can be expected to continue to do so for greater insight into natural processes and their informed exploitation in biotechnologies.

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Section: Redox Potentialsmentioning

confidence: 99%

Multi-haem cytochromes inShewanella oneidensisMR-1: structures, functions and opportunities

Breuer

Rosso

Blumberger

et al. 2015

J. R. Soc. Interface.

224

186

View full text Add to dashboard Cite

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“…large subunit small subunit -hydrogenases and the location of the prosthetic groups. The reduction potentials (at pH 7) of the groups are approximately K100, K30, K345 and K290 mV for the Ni ion (Ni 3C/2C transition in unready enzyme), the medial Fe-S cluster ([3Fe-4S] 1C/0 ) and the proximal and distal Fe-S clusters ([4Fe-4S] 2C/1C ), respectively (Teixeira et al 1989;Coremans et al 1992). The reduction potential of the Ni 3C/2C transition in active enzyme (K390 mV) is much lower than that in unready enzyme owing to the tight binding of a hydride in active enzyme.…”

Section: Information From Spectroscopymentioning

confidence: 99%

[NiFe]-hydrogenases: spectroscopic and electrochemical definition of reactions and intermediates

Armstrong

Albracht

2005

Phil. Trans. R. Soc. A.

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Production and usage of di-hydrogen, H2, in micro-organisms is catalysed by highly active, 'ancient' metalloenzymes known as hydrogenases. Based on the number and identity of metal atoms in their active sites, hydrogenases fall into three main classes, [NiFe]-, [FeFe]- and [Fe]-. All contain the unusual ligand CO (and in most cases CN- as well) making them intriguing examples of 'organometallic' cofactors. These ligands render the active sites superbly 'visible' using infrared spectroscopy, which complements the use of electron paramagnetic resonance spectroscopy in studying mechanisms and identifying intermediates. Hydrogenases are becoming a focus of attention for research into future energy technologies, not only H2 production but also H2 oxidation in fuel cells. Hydrogenases immobilized on electrodes exhibit high electrocatalytic activity, providing not only an important new technique for their investigation, but also a basis for novel fuel cells either using the enzyme itself, or inspired synthetic catalysts. Favourable comparisons have been made with platinum electrocatalysts, an advantage of enzymes being their specificity for H2 and tolerance of CO. A challenge for exploiting hydrogenases is their sensitivity to O2, but some organisms are known to produce enzymes that overcome this problem by subtle alterations of the active site and gas access channels.

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“…We have recently demonstrated that, in the CO-related structures, the Ni and Sg(Cys546) atoms show flexibility, which suggested that these two atoms play a key role during the initial H 2 binding process (Ogata et al, 2002). [NiFe] hydrogenase also possesses one [Fe 3 S 4 ] 1+/0 cluster with a relatively high midpoint potential (270 mV) and two [Fe 4 S 4 ] 2+/1+ clusters with lower midpoint potentials (2290 and 2340 mV, respectively) (Higuchi et al, 1997;Teixeira et al, 1989;Volbeda et al, 1995), and the EPR signal of the oxidized [Fe 3 S 4 ] + cluster is detected at g = 2.01 at low temperatures (Albracht et al, 1983;Cammack et al, 1987).…”

Section: Introductionmentioning

confidence: 99%

Activation Process of [NiFe] Hydrogenase Elucidated by High-Resolution X-Ray Analyses: Conversion of the Ready to the Unready State

et al. 2005

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Hydrogenases catalyze oxidoreduction of molecular hydrogen and have potential applications for utilizing dihydrogen as an energy source. [NiFe] hydrogenase has two different oxidized states, Ni-A (unready, exhibits a lag phase in reductive activation) and Ni-B (ready). We have succeeded in converting Ni-B to Ni-A with the use of Na 2 S and O 2 and determining the high-resolution crystal structures of both states. Ni-B possesses a monatomic nonprotein bridging ligand at the Ni-Fe active site, whereas Ni-A has a diatomic species. The terminal atom of the bridging species of Ni-A occupies a similar position as C of the exogenous CO in the CO complex (inhibited state). The common features of the enzyme structures at the unready (Ni-A) and inhibited (CO complex) states are proposed. These findings provide useful information on the design of new systems of biomimetic dihydrogen production and fuel cell devices.

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Redox Intermediates of Desulfovibrio gigas [NiFe] Hydrogenase Generated Under Hydrogen

Cited by 168 publications

References 63 publications

Multi-haem cytochromes inShewanella oneidensisMR-1: structures, functions and opportunities

Multi-haem cytochromes inShewanella oneidensisMR-1: structures, functions and opportunities

[NiFe]-hydrogenases: spectroscopic and electrochemical definition of reactions and intermediates

Activation Process of [NiFe] Hydrogenase Elucidated by High-Resolution X-Ray Analyses: Conversion of the Ready to the Unready State

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