Carbon Monoxide as an Intrinsic Ligand to Iron in the Active Site of the Iron−Sulfur-Cluster-Free Hydrogenase H2-Forming Methylenetetrahydromethanopterin Dehydrogenase As Revealed by Infrared Spectroscopy-Reference-Cited by-同舟云学术

Carbon Monoxide as an Intrinsic Ligand to Iron in the Active Site of the Iron−Sulfur-Cluster-Free Hydrogenase H2-Forming Methylenetetrahydromethanopterin Dehydrogenase As Revealed by Infrared Spectroscopy

Published:2004-10-06 Issue:43 Volume:126 Page:14239-14248
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Lyon Erica J.¹,Shima Seigo¹,Boecher Reinhard¹,Thauer Rudolf K.¹,Grevels Friedrich-Wilhelm¹,Bill Eckhard¹,Roseboom Winfried¹,Albracht Simon P. J.¹

Affiliation:

1. Contribution from the Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Strasse, D-35043 Marburg, Germany, Max Planck Institute for Bioinorganic Chemistry, Stift Strasse 34-36, D-45470 Mülheim an der Ruhr, Germany, and Biochemistry, Swammerdam Institute for Life Sciences, University of Amsterdam, Plantage Muidergracht 12, NL-1018 TV Amsterdam, The Netherlands

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja046818s

Reference50 articles.

1. Infrared Studies on the Interaction of Carbon Monoxide with Divalent Nickel in Hydrogenase from Chromatium vinosum

2. Infrared-Detectable Group Senses Changes in Charge Density on the Nickel Center in Hydrogenase from Chromatium vinosum

3. Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas

4. Carbon Monoxide and Cyanide as Intrinsic Ligands to Iron in the Active Site of [NiFe]-Hydrogenases

5. Biological activition of hydrogen

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