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Title: X-ray absorption spectroscopy of the corrinoid/iron-sulfur potein involved in acetyl coenzyme A synthesis by Clostridium thermoaceticum

Journal Article · · Journal of the American Chemical Society; (United States)
DOI:https://doi.org/10.1021/ja00059a007· OSTI ID:5981186
;  [1]; ;  [2]
  1. Yeshiva Univ., Bronx, NY (United States)
  2. Univ. of Nebraska, Lincoln (United States)

The corrinoid/iron-sulfur protein (C/Fe-SP) from Clostridium thermoaceticum is an 88 kDa [alpha][beta]-dimer that cycles between a Co(I) and methyl-Co(III) form as it transfers a methyl group from methyltetrahydrofolate (methyl-H[sub 4]folate) to carbon monoxide dehydrogenase. Extended X-ray absorption fine structure (EXAFS) and X-ray edge spectroscopy of the as-isolated C/Fe-SP indicates that the inactive Co(II) state of the corrinoid has a four-coordinate distorted square-planar structure. To the authors' knowledge, this is the first observation of a four-coordinate Co(II) corrinoid. This unusual coordination state would be expected to poise the Co(II) state of the C/Fe-SP for facile reduction to four-coordinate Co(I), which is the active nucleophile that acts as the acceptor of the methyl group of methyl-H[sub 4]folate. Additionally, the first-derivative X-ray edge spectra for both the methyl-Co(III) and Co(II) forms of the C/Fe-SP show an unexpected shift to lower energy when compared to analogous free cobalamins indicating a potential role for the protein in mediating electronic as well as structural properties of the enzyme bound methylcobamide. 42 refs., 6 figs., 3 tabs.

DOE Contract Number:
AC02-76CH00016
OSTI ID:
5981186
Journal Information:
Journal of the American Chemical Society; (United States), Vol. 115:6; ISSN 0002-7863
Country of Publication:
United States
Language:
English