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This article has been retracted

Science 27 October 1995:
Vol. 270. no. 5236, pp. 628 - 630
DOI: 10.1126/science.270.5236.628
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Reports

A Methylnickel Intermediate in a Bimetallic Mechanism of Acetyl-Coenzyme A Synthesis by Anaerobic Bacteria

Manoj Kumar,  Di Qiu,  Thomas G. Spiro (1),  Stephen W. Ragsdale (1)

Resonance Raman (RR) spectroscopy was used to identify a methylnickel adduct ( = 422 wave numbers) of carbon monoxide dehydrogenase (CODH) from Clostridium thermoaceticum. Formed at a nickel/iron-sulfur cluster on CODH called center A, the methylnickel species is the precursor of the methyl group of acetyl-coenzyme A in an anaerobic pathway of carbon monoxide or carbon dioxide fixation. Rapid kinetic and RR studies demonstrated that methylation of nickel occurs by heterolysis of the methyl-cobalt bond ( = 429 wave numbers) of a methylated corrinoid/iron-sulfur protein. In combination with the earlier finding of an iron-carbonyl adduct at center A, detection of the methylnickel intermediate establishes a bimetallic mechanism for acetyl-coenzyme A synthesis.


M. Kumar and S. W. Ragsdale, Department of Biochemistry, Beadle Center, University of Nebraska, Lincoln, NE 68588-0664, USA.
D. Qiu and T. G. Spiro, Department of Chemistry, Princeton University, Princeton, NJ 08544, USA.
(1) To whom correspondence should be addressed.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The Role of an Iron-Sulfur Cluster in an Enzymatic Methylation Reaction. METHYLATION OF CO DEHYDROGENASE/ACETYL-CoA SYNTHASE BY THE METHYLATED CORRINOID IRON-SULFUR PROTEIN.
S. Menon and S. W. Ragsdale (1999)
J. Biol. Chem. 274, 11513-11518
   Abstract »    Full Text »    PDF »
Activated Acetic Acid by Carbon Fixation on (Fe,Ni)S Under Primordial Conditions.
C. Huber and G. Wächtershäuser (1997)
Science 276, 245-247
   Abstract »    Full Text »
Metal-Carbon Bonds in Nature.
J. A. Kovacs, S. C. Shoner, and J. J. Ellison (1995)
Science 270, 587-588
   Abstract »    PDF »


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