CO-induced structural rearrangement of the C cluster in Carboxydothermus hydrogenoformans CO dehydrogenase - Evidence from Ni K-edge X-ray absorption spectroscopy?

Weiwei Gu, Javier Seravalli, Stephen W. Ragsdale, Stephen P. Cramer

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

We have examined the C cluster in type II CO dehydrogenase (CODH) from Carboxydothermus hydrogenformans using Ni K-edge X-ray absorption near edge spectroscopy and extended X-ray absorption fine structure (EXAFS) spectroscopy. The enzyme was studied under three conditions: "as-isolated" and after treatment with CO or Ti1II. The shape of the Ni K-edge changes slightly between the different conditions, but no significant edge shift is seen, suggesting that the C cluster contains NiII in both forms. The Ni EXAFS of as-isolated CODH can be simulated with 4 Ni-S interactions at 2.20 Å with a large spread in distances. A light atom (C, N, O) is not required to fit the spectrum. After CO treatment, significant changes are observed in the EXAFS. A new feature appears at ∼-2.7 Å; this component is consistent with a Ni-Fe interaction. The average Ni-S distance also expands to ∼2.25 Å. The changes between the two forms suggest that the active site (C cluster) undergoes structural rearrangement after CO treatment, and the observed changes help reconcile the two different crystal structures. The implications of the structural change for the enzyme activation and mechanism are discussed.

Original languageEnglish (US)
Pages (from-to)9029-9035
Number of pages7
JournalBiochemistry
Volume43
Issue number28
DOIs
StatePublished - Jul 20 2004

Fingerprint

carbon monoxide dehydrogenase
X-Ray Absorption Spectroscopy
X ray absorption spectroscopy
X ray absorption
Carbon Monoxide
X-Rays
Extended X ray absorption fine structure spectroscopy
Enzyme Activation
Enzymes
Catalytic Domain
Spectrum Analysis
Crystal structure
Chemical activation
Spectroscopy
Light
Atoms

ASJC Scopus subject areas

  • Biochemistry

Cite this

CO-induced structural rearrangement of the C cluster in Carboxydothermus hydrogenoformans CO dehydrogenase - Evidence from Ni K-edge X-ray absorption spectroscopy? / Gu, Weiwei; Seravalli, Javier; Ragsdale, Stephen W.; Cramer, Stephen P.

In: Biochemistry, Vol. 43, No. 28, 20.07.2004, p. 9029-9035.

Research output: Contribution to journalArticle

@article{508390b7d87446e09f1188de2d8880f7,
title = "CO-induced structural rearrangement of the C cluster in Carboxydothermus hydrogenoformans CO dehydrogenase - Evidence from Ni K-edge X-ray absorption spectroscopy?",
abstract = "We have examined the C cluster in type II CO dehydrogenase (CODH) from Carboxydothermus hydrogenformans using Ni K-edge X-ray absorption near edge spectroscopy and extended X-ray absorption fine structure (EXAFS) spectroscopy. The enzyme was studied under three conditions: {"}as-isolated{"} and after treatment with CO or Ti1II. The shape of the Ni K-edge changes slightly between the different conditions, but no significant edge shift is seen, suggesting that the C cluster contains NiII in both forms. The Ni EXAFS of as-isolated CODH can be simulated with 4 Ni-S interactions at 2.20 {\AA} with a large spread in distances. A light atom (C, N, O) is not required to fit the spectrum. After CO treatment, significant changes are observed in the EXAFS. A new feature appears at ∼-2.7 {\AA}; this component is consistent with a Ni-Fe interaction. The average Ni-S distance also expands to ∼2.25 {\AA}. The changes between the two forms suggest that the active site (C cluster) undergoes structural rearrangement after CO treatment, and the observed changes help reconcile the two different crystal structures. The implications of the structural change for the enzyme activation and mechanism are discussed.",
author = "Weiwei Gu and Javier Seravalli and Ragsdale, {Stephen W.} and Cramer, {Stephen P.}",
year = "2004",
month = "7",
day = "20",
doi = "10.1021/bi036104e",
language = "English (US)",
volume = "43",
pages = "9029--9035",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "28",

}

TY - JOUR

T1 - CO-induced structural rearrangement of the C cluster in Carboxydothermus hydrogenoformans CO dehydrogenase - Evidence from Ni K-edge X-ray absorption spectroscopy?

AU - Gu, Weiwei

AU - Seravalli, Javier

AU - Ragsdale, Stephen W.

AU - Cramer, Stephen P.

PY - 2004/7/20

Y1 - 2004/7/20

N2 - We have examined the C cluster in type II CO dehydrogenase (CODH) from Carboxydothermus hydrogenformans using Ni K-edge X-ray absorption near edge spectroscopy and extended X-ray absorption fine structure (EXAFS) spectroscopy. The enzyme was studied under three conditions: "as-isolated" and after treatment with CO or Ti1II. The shape of the Ni K-edge changes slightly between the different conditions, but no significant edge shift is seen, suggesting that the C cluster contains NiII in both forms. The Ni EXAFS of as-isolated CODH can be simulated with 4 Ni-S interactions at 2.20 Å with a large spread in distances. A light atom (C, N, O) is not required to fit the spectrum. After CO treatment, significant changes are observed in the EXAFS. A new feature appears at ∼-2.7 Å; this component is consistent with a Ni-Fe interaction. The average Ni-S distance also expands to ∼2.25 Å. The changes between the two forms suggest that the active site (C cluster) undergoes structural rearrangement after CO treatment, and the observed changes help reconcile the two different crystal structures. The implications of the structural change for the enzyme activation and mechanism are discussed.

AB - We have examined the C cluster in type II CO dehydrogenase (CODH) from Carboxydothermus hydrogenformans using Ni K-edge X-ray absorption near edge spectroscopy and extended X-ray absorption fine structure (EXAFS) spectroscopy. The enzyme was studied under three conditions: "as-isolated" and after treatment with CO or Ti1II. The shape of the Ni K-edge changes slightly between the different conditions, but no significant edge shift is seen, suggesting that the C cluster contains NiII in both forms. The Ni EXAFS of as-isolated CODH can be simulated with 4 Ni-S interactions at 2.20 Å with a large spread in distances. A light atom (C, N, O) is not required to fit the spectrum. After CO treatment, significant changes are observed in the EXAFS. A new feature appears at ∼-2.7 Å; this component is consistent with a Ni-Fe interaction. The average Ni-S distance also expands to ∼2.25 Å. The changes between the two forms suggest that the active site (C cluster) undergoes structural rearrangement after CO treatment, and the observed changes help reconcile the two different crystal structures. The implications of the structural change for the enzyme activation and mechanism are discussed.

UR - http://www.scopus.com/inward/record.url?scp=3142777049&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=3142777049&partnerID=8YFLogxK

U2 - 10.1021/bi036104e

DO - 10.1021/bi036104e

M3 - Article

VL - 43

SP - 9029

EP - 9035

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 28

ER -