O2-stable membrane-bound [NiFe]hydrogenase from a newly isolated Citrobacter sp. S-77

Eguchi, Shigenobu; Yoon, Ki Seok; Ogo, Seiji

doi:10.1016/j.jbiosc.2012.05.018

Cited by 19 publications

(12 citation statements)

References 35 publications

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“…When calculating the difference spectra of H 2 -reduced minus oxidized state, the spectrum showed α-, β-, and γ-absorption peaks at 561, 530, and 427 nm, respectively ( Figure 7B ). These spectral properties correspond to absorption spectra of b -type cytochromes (Yoon et al, 2008; Eguchi et al, 2012). …”

Section: Resultsmentioning

confidence: 85%

The NiFe Hydrogenases of the Tetrachloroethene-Respiring Epsilonproteobacterium Sulfurospirillum multivorans: Biochemical Studies and Transcription Analysis

Kruse¹,

Goris²,

Wolf³

et al. 2017

Front. Microbiol.

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The organohalide-respiring Epsilonproteobacterium Sulfurospirillum multivorans is able to grow with hydrogen as electron donor and with tetrachloroethene (PCE) as electron acceptor; PCE is reductively dechlorinated to cis-1,2-dichloroethene. Recently, a genomic survey revealed the presence of four gene clusters encoding NiFe hydrogenases in its genome, one of which is presumably periplasmic and membrane-bound (MBH), whereas the remaining three are cytoplasmic. To explore the role and regulation of the four hydrogenases, quantitative real-time PCR and biochemical studies were performed with S. multivorans cells grown under different growth conditions. The large subunit genes of the MBH and of a cytoplasmic group 4 hydrogenase, which is assumed to be membrane-associated, show high transcript levels under nearly all growth conditions tested, pointing toward a constitutive expression in S. multivorans. The gene transcripts encoding the large subunits of the other two hydrogenases were either not detected at all or only present at very low amounts. The presence of MBH under all growth conditions tested, even with oxygen as electron acceptor under microoxic conditions, indicates that MBH gene transcription is not regulated in contrast to other facultative hydrogen-oxidizing bacteria. The MBH showed quinone-reactivity and a characteristic UV/VIS spectrum implying a cytochrome b as membrane-integral subunit. Cell extracts of S. multivorans were subjected to native polyacrylamide gel electrophoresis (PAGE) and hydrogen oxidizing activity was tested by native staining. Only one band was detected at about 270 kDa in the particulate fraction of the extracts, indicating that there is only one hydrogen-oxidizing enzyme present in S. multivorans. An enrichment of this enzyme and SDS PAGE revealed a subunit composition corresponding to that of the MBH. From these findings we conclude that the MBH is the electron-donating enzyme system in the PCE respiratory chain. The roles for the other three hydrogenases remain unproven. The group 4 hydrogenase might be involved in hydrogen production upon fermentative growth.

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Section: Resultsmentioning

confidence: 85%

The NiFe Hydrogenases of the Tetrachloroethene-Respiring Epsilonproteobacterium Sulfurospirillum multivorans: Biochemical Studies and Transcription Analysis

Kruse¹,

Goris²,

Wolf³

et al. 2017

Front. Microbiol.

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“…Aso in Japan, contains a [NiFe]H 2 ase ([NiFe] S77 ) that can be used as an electrode catalyst in fuel cells [20]. Hydrogen half-cells using [NiFe] S77 as the anode catalyst exhibit H 2 activation potential that is 637 times greater than that of Pt per unit of weight (Fig.…”

Section: Application To Fuel Cellsmentioning

confidence: 99%

H2 and O2 activation by [NiFe]hydrogenases – Insights from model complexes

Ogo

2017

Coordination Chemistry Reviews

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“…Earlier, the same group had discovered a unique [NiFe]hydrogenase from Citrobacter sp. S‐77 ([NiFe]S 77 ) . This [NiFe]S 77 is highly active and stable in O 2 , and also its mass activity was found to be 637 times higher when compared with Pt in a hydrogen half‐cell.…”

Section: Molecular Catalysts As the Anode In Complete Fuel Cellsmentioning

confidence: 99%

Design and Integration of Molecular‐Type Catalysts in Fuel‐Cell Technology

et al. 2018

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The ORCID identification number(s) for the author(s) of this article can be found under https://doi.org/10.1002/smtd.201800059.The field of molecular electrocatalysis research includes a wide range of emerging technologies that utilize molecular catalysts to catalyze anodic and/ or cathodic reactions within a fuel-cell setup, and has developed greatly in the last 10 years. Although the vast majority of fuel cells utilize noble metals as catalysts, several systems have been recently developed that are based on molecular catalysts. The focus here is on the integration of molecular catalysts in a fuel-cell setup, which is contextualized, and which is named as "fuel-cell-based molecular-type catalysts" here. The latter utilize a wide variety of chemical compounds, such as organometallics and organic or bioinspired compounds, to harvest chemical energy to generate current. Here, the stateof-the-art for all molecular catalysts that convert chemical energy in a fuel-cell setup is discussed and a novel classification system is presented to illustrate how molecular catalysts integrate into the broad field of fuel cells. The current performance of molecular catalysts in systems that use different fuels is summarized, and finally, for the first time, the achievable power outputs of fuel cells using uniquely molecular catalysts are presented. Molecular Catalysts

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O2-stable membrane-bound [NiFe]hydrogenase from a newly isolated Citrobacter sp. S-77

Cited by 19 publications

References 35 publications

The NiFe Hydrogenases of the Tetrachloroethene-Respiring Epsilonproteobacterium Sulfurospirillum multivorans: Biochemical Studies and Transcription Analysis

The NiFe Hydrogenases of the Tetrachloroethene-Respiring Epsilonproteobacterium Sulfurospirillum multivorans: Biochemical Studies and Transcription Analysis

H2 and O2 activation by [NiFe]hydrogenases – Insights from model complexes

Design and Integration of Molecular‐Type Catalysts in Fuel‐Cell Technology

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