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Structural diversity of F/sub 430/ from methanobacterium thermoautotrophicum. A nickel x-ray absorption spectroscopic study

Journal Article · · J. Am. Chem. Soc.; (United States)
DOI:https://doi.org/10.1021/ja00271a060· OSTI ID:5430146

Nickel metalloenzymes have been found in all methane-producing bacteria examined. Two hydrogenases from Methanobacterium thermoautotrophicum contain nickel which has been shown to be coordinated by S-containing ligands in one form. A compound called F/sub 430/ has been isolated from M. thermoautotrophicum, strain ..delta..H, and has been identified as the Ni-containing prosthetic group in protein component C of the S-methyl coenzyme-M reductase system. F/sub 430/ has been established to have a Ni(II)-tetrapyrrole structure, constituting the only known biological example of nickel in a tetrahydro reduced corphine. The detailed mechanistic role of F/sub 430/ in methyl group reduction has not been identified. We report here a Ni x-ray absorption spectroscopic (XAS) study of several forms of F/sub 430/ and component C isolated from M. thermoautotrophicum, strain ..delta..H. These preliminary results indicate that free F/sub 430/ is structurally distinct from the F/sub 430/-containing protein. Also, depending upon the conditions used, extraction of F/sub 430/ from the protein yields at least two structurally distinct forms, one similar to that in the intact protein and one similar to free F/sub 430/. Analysis of the extended x-ray absorption fine structure (EXAFS) data and comparison with a number of structurally characterized Ni(II) complexes provide evidence that the flexibility of the tetrapyrrole is responsible for the different structural forms.

Research Organization:
Univ. of Illinois, Urbana
OSTI ID:
5430146
Journal Information:
J. Am. Chem. Soc.; (United States), Journal Name: J. Am. Chem. Soc.; (United States) Vol. 108:11; ISSN JACSA
Country of Publication:
United States
Language:
English