Unambiguous identification of the nickel EPR signal in 61Ni-enriched Desulfovibrio gigas hydrogenase

Moura, José J. G.; Moura, Isabel; Huynh, B.H.; Krüger, Hans‐Jörg; Teixeira, Miguel; DuVarney, R. C.; Dervartanian, D.V.; Xavier, António V.; Peck, Harry D.; LeGall, Jean

doi:10.1016/s0006-291x(82)80060-0

Cited by 111 publications

(68 citation statements)

References 10 publications

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“…Eidsness et al [56,57] concluded for the D. gigas enzyme that the coordination would be tetragonally-distorted octahedral or trigonalbipyramidal, in line with earlier conclusions based on the EPR spectra of Ni(III) in several hydrogenases [7,29,144]. Maroney and coworkers came to a similar conclusion from X-ray absorption studies on the T. roseopersicina enzyme [18,136,137,224,225].…”

Section: Sulphur Oxygen and Nitrogensupporting

confidence: 55%

“…Therefore the signal was ascribed to nickel. It was first reported by Moura et al [144] in the D. gigas enzyme and interpreted by these investigators as another form of Ni(III). Being the third signal detected for nickel in hydrogenases, it is often called Ni-C (gxyz = 2.19, 2.16, 2.02).…”

Section: Redox Behaviour Of Ni=(i)h E ('Ni-c')mentioning

confidence: 89%

“…The Ni-C signal in the enzyme from C. vinosum has also been observed at room temperature (Chen, M. and Albracht, S.P.J., unpublished observations), excluding any freezing artifact. The unpaired spin causing this signal showed considerable nickel-hyperfine interaction in 61Ni-enriched preparations [33,112,144]. Therefore the signal was ascribed to nickel.…”

Section: Redox Behaviour Of Ni=(i)h E ('Ni-c')mentioning

confidence: 90%

“…Once over the barrier ('reductive activation') all nickel hydrogenases examined so far show the Ni-C EPR signal [12,29,62,112,144,176,[196][197][198]206]. The Ni-C signal in the enzyme from C. vinosum has also been observed at room temperature (Chen, M. and Albracht, S.P.J., unpublished observations), excluding any freezing artifact.…”

Section: Redox Behaviour Of Ni=(i)h E ('Ni-c')mentioning

confidence: 92%

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Nickel hydrogenases: in search of the active site

Albracht

1994

Biochimica et Biophysica Acta (BBA) - Bioenergetics

470

479

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Section: Sulphur Oxygen and Nitrogensupporting

confidence: 55%

Section: Redox Behaviour Of Ni=(i)h E ('Ni-c')mentioning

confidence: 89%

Section: Redox Behaviour Of Ni=(i)h E ('Ni-c')mentioning

confidence: 90%

Section: Redox Behaviour Of Ni=(i)h E ('Ni-c')mentioning

confidence: 92%

See 2 more Smart Citations

Nickel hydrogenases: in search of the active site

Albracht

1994

Biochimica et Biophysica Acta (BBA) - Bioenergetics

470

479

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“…, Fe 2? ) [54,55]. During this incubation period, the EPR signals assigned to the inactive state (namely Ni-A) disappear and are slowly converted to another species, named Ni-C (Ni 3?…”

Section: Ni-fe Hydrogenasementioning

confidence: 99%

Enzymatic activity mastered by altering metal coordination spheres

2008

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Metalloenzymes control enzymatic activity by changing the characteristics of the metal centers where catalysis takes place. The conversion between inactive and active states can be tuned by altering the coordination number of the metal site, and in some cases by an associated conformational change. These processes will be illustrated using heme proteins (cytochrome c nitrite reductase, cytochrome c peroxidase and cytochrome cd 1 nitrite reductase), non-heme proteins (superoxide reductase and [NiFe]-hydrogenase), and copper proteins (nitrite and nitrous oxide reductases) as examples. These examples catalyze electron transfer reactions that include atom transfer, abstraction and insertion.

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Nickel–Iron Hydrogenases

Frey

Volbeda

2004

Handbook of Metalloproteins

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Ni–Fe hydrogenases catalyze the cleavage or the production of the most simple of chemical compounds, molecular hydrogen. This review provides an overview of the literature on these enzymes that has been published before the year 2000. On the basis of atomic models plausible pathways of substrates and products are described, including a hydrophobic tunnel network for H 2 diffusion, a suitable arrangement of three iron–sulfur clusters for electron transfer, a network of buried water molecules, and a magnesium site that could be involved in proton transfer. A combination of protein crystallography, electron paramagnetic resonance, and Fourier transform infrared spectroscopic studies has allowed the elucidation of the unique architecture of the active site. This consists of a thiolate‐coordinated Ni–Fe unit involving one carbon monoxide and two cyanide ligands to the iron, leaving two metal coordination sites available for substrate binding. Understanding the catalytic mechanism of these fascinating enzymes might be helpful for the development of cheap catalysts for fuel cells working on H 2 or of cheaper production methods for this clean fuel.

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Unambiguous identification of the nickel EPR signal in 61Ni-enriched Desulfovibrio gigas hydrogenase

Cited by 111 publications

References 10 publications

Nickel hydrogenases: in search of the active site

Nickel hydrogenases: in search of the active site

Enzymatic activity mastered by altering metal coordination spheres

Nickel–Iron Hydrogenases

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