Catalytic cycle of cytochrome-c3 hydrogenase, a [NiFe]-enzyme, deduced from the structures of the enzyme and the enzyme mimic

Tatsuhiko Yagi, Seiji Ogo, Yoshiki Higuchi

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Hydrogenases catalyze uptake and production of H2. Heterolytic cleavage of H2 bound on [NiFe]-hydrogenase (E) produces two unequal H species to form E:HaHb, where Ha and Hb behave differently. The structures of various states of the enzyme established by crystallography and spectroscopy were used to construct a catalytic cycle of the enzyme. The Ni-Fe center of the active enzyme has the Ni-Fe bridging site vacant. The enzyme is suggested to bind H2 either at Ni or Fe atom. In E:HaHb, Ha is considered to be a protein-bound hydron (proton or deuteron) at the entrance to the hydrophobic gas tunnel. The structure of a synthetic hydrogenase-mimic suggests Hb to be the 6th ligand to Fe. Two successive one-electron processes from E:HaHb complete the catalytic cycle of H2 uptake. The reverse of the cycle operates in the H2 production. The proposed catalytic cycle is consistent with the kinetic, crystallographic and spectroscopic studies.

Original languageEnglish
Pages (from-to)18543-18550
Number of pages8
JournalInternational Journal of Hydrogen Energy
Volume39
Issue number32
DOIs
Publication statusPublished - Oct 31 2014

Fingerprint

cytochromes
enzymes
Enzymes
Proteins
cycles
Crystallography
entrances
crystallography
deuterons
tunnels
cleavage
Tunnels
Protons
Ligands
Spectroscopy
proteins
Atoms
ligands
Kinetics
protons

All Science Journal Classification (ASJC) codes

  • Renewable Energy, Sustainability and the Environment
  • Fuel Technology
  • Condensed Matter Physics
  • Energy Engineering and Power Technology

Cite this

Catalytic cycle of cytochrome-c3 hydrogenase, a [NiFe]-enzyme, deduced from the structures of the enzyme and the enzyme mimic. / Yagi, Tatsuhiko; Ogo, Seiji; Higuchi, Yoshiki.

In: International Journal of Hydrogen Energy, Vol. 39, No. 32, 31.10.2014, p. 18543-18550.

Research output: Contribution to journalArticle

@article{877477fc85184005b21b9bd754acea98,
title = "Catalytic cycle of cytochrome-c3 hydrogenase, a [NiFe]-enzyme, deduced from the structures of the enzyme and the enzyme mimic",
abstract = "Hydrogenases catalyze uptake and production of H2. Heterolytic cleavage of H2 bound on [NiFe]-hydrogenase (E) produces two unequal H species to form E:HaHb, where Ha and Hb behave differently. The structures of various states of the enzyme established by crystallography and spectroscopy were used to construct a catalytic cycle of the enzyme. The Ni-Fe center of the active enzyme has the Ni-Fe bridging site vacant. The enzyme is suggested to bind H2 either at Ni or Fe atom. In E:HaHb, Ha is considered to be a protein-bound hydron (proton or deuteron) at the entrance to the hydrophobic gas tunnel. The structure of a synthetic hydrogenase-mimic suggests Hb to be the 6th ligand to Fe. Two successive one-electron processes from E:HaHb complete the catalytic cycle of H2 uptake. The reverse of the cycle operates in the H2 production. The proposed catalytic cycle is consistent with the kinetic, crystallographic and spectroscopic studies.",
author = "Tatsuhiko Yagi and Seiji Ogo and Yoshiki Higuchi",
year = "2014",
month = "10",
day = "31",
doi = "10.1016/j.ijhydene.2013.12.174",
language = "English",
volume = "39",
pages = "18543--18550",
journal = "International Journal of Hydrogen Energy",
issn = "0360-3199",
publisher = "Elsevier Limited",
number = "32",

}

TY - JOUR

T1 - Catalytic cycle of cytochrome-c3 hydrogenase, a [NiFe]-enzyme, deduced from the structures of the enzyme and the enzyme mimic

AU - Yagi, Tatsuhiko

AU - Ogo, Seiji

AU - Higuchi, Yoshiki

PY - 2014/10/31

Y1 - 2014/10/31

N2 - Hydrogenases catalyze uptake and production of H2. Heterolytic cleavage of H2 bound on [NiFe]-hydrogenase (E) produces two unequal H species to form E:HaHb, where Ha and Hb behave differently. The structures of various states of the enzyme established by crystallography and spectroscopy were used to construct a catalytic cycle of the enzyme. The Ni-Fe center of the active enzyme has the Ni-Fe bridging site vacant. The enzyme is suggested to bind H2 either at Ni or Fe atom. In E:HaHb, Ha is considered to be a protein-bound hydron (proton or deuteron) at the entrance to the hydrophobic gas tunnel. The structure of a synthetic hydrogenase-mimic suggests Hb to be the 6th ligand to Fe. Two successive one-electron processes from E:HaHb complete the catalytic cycle of H2 uptake. The reverse of the cycle operates in the H2 production. The proposed catalytic cycle is consistent with the kinetic, crystallographic and spectroscopic studies.

AB - Hydrogenases catalyze uptake and production of H2. Heterolytic cleavage of H2 bound on [NiFe]-hydrogenase (E) produces two unequal H species to form E:HaHb, where Ha and Hb behave differently. The structures of various states of the enzyme established by crystallography and spectroscopy were used to construct a catalytic cycle of the enzyme. The Ni-Fe center of the active enzyme has the Ni-Fe bridging site vacant. The enzyme is suggested to bind H2 either at Ni or Fe atom. In E:HaHb, Ha is considered to be a protein-bound hydron (proton or deuteron) at the entrance to the hydrophobic gas tunnel. The structure of a synthetic hydrogenase-mimic suggests Hb to be the 6th ligand to Fe. Two successive one-electron processes from E:HaHb complete the catalytic cycle of H2 uptake. The reverse of the cycle operates in the H2 production. The proposed catalytic cycle is consistent with the kinetic, crystallographic and spectroscopic studies.

UR - http://www.scopus.com/inward/record.url?scp=84908256481&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84908256481&partnerID=8YFLogxK

U2 - 10.1016/j.ijhydene.2013.12.174

DO - 10.1016/j.ijhydene.2013.12.174

M3 - Article

AN - SCOPUS:84908256481

VL - 39

SP - 18543

EP - 18550

JO - International Journal of Hydrogen Energy

JF - International Journal of Hydrogen Energy

SN - 0360-3199

IS - 32

ER -