Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1985 Mar;82(5):1364–1366. doi: 10.1073/pnas.82.5.1364

Stereochemical studies of a selenium-containing hydrogenase from Methanococcus vannielii: determination of the absolute configuration of C-5 chirally labeled dihydro-8-hydroxy-5-deazaflavin cofactor.

S Yamazaki, L Tsai, T C Stadtman, T Teshima, A Nakaji, T Shiba
PMCID: PMC397261  PMID: 3883357

Abstract

Reduction of 7,8-didemethyl-8-hydroxy-[5-2H]-5-deazariboflavin by the selenium-containing hydrogenase from Methanococcus vannielii gave a C-5 chirally labeled 1,5-dihydro derivative. The absolute configuration of the chiral label was shown to be (R) by comparison of the chemically degraded product with authentic samples of known absolute configurations. Therefore, the steric course of the enzymic reactions involving the 8-hydroxy-5-deazaflavin cofactor can be defined as follows: (a) reduction occurs on the si face of the 5-deazaflavin molecule; (b) oxidation proceeds by the abstraction of the pro-S hydrogen at C-5 of the 1,5-dihydro-5-deazaflavin. Thus, the selenium-containing hydrogenase and 8-hydroxy-5-deazaflavin-dependent NADP+ reductase from M. vannielii are si face specific.

Full text

PDF
1364

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Eirich L. D., Vogels G. D., Wolfe R. S. Proposed structure for coenzyme F420 from Methanobacterium. Biochemistry. 1978 Oct 31;17(22):4583–4593. doi: 10.1021/bi00615a002. [DOI] [PubMed] [Google Scholar]
  2. Ellefson W. L., Wolfe R. S. Role of component C in the methylreductase system of Methanobacterium. J Biol Chem. 1980 Sep 25;255(18):8388–8389. [PubMed] [Google Scholar]
  3. Jones J. B., Stadtman T. C. Reconstitution of a formate-NADP+ oxidoreductase from formate dehydrogenase and a 5-deazaflavin-linked NADP+ reductase isolated from Methanococcus vannielii. J Biol Chem. 1980 Feb 10;255(3):1049–1053. [PubMed] [Google Scholar]
  4. Tzeng S. F., Wolfe R. S., Bryant M. P. Factor 420-dependent pyridine nucleotide-linked hydrogenase system of Methanobacterium ruminantium. J Bacteriol. 1975 Jan;121(1):184–191. doi: 10.1128/jb.121.1.184-191.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Tzing S. F., Bryant M. P., Wolfe R. S. Factor 420-dependent pyridine nucleotide-linked formate metabolism of Methanobacterium ruminantium. J Bacteriol. 1975 Jan;121(1):192–196. doi: 10.1128/jb.121.1.192-196.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Yamazaki S. A selenium-containing hydrogenase from Methanococcus vannielii. Identification of the selenium moiety as a selenocysteine residue. J Biol Chem. 1982 Jul 25;257(14):7926–7929. [PubMed] [Google Scholar]
  7. Yamazaki S., Tsai L. Purification and properties of 8-hydroxy-5-deazaflavin-dependent NADP+ reductase from Methanococcus vannielii. J Biol Chem. 1980 Jul 10;255(13):6462–6465. [PubMed] [Google Scholar]
  8. Yamazaki S., Tsai L., Stadtman T. C. Analogues of 8-hydroxy-5-deazaflavin cofactor: relative activity as substrates for 8-hydroxy-5-deazaflavin-dependent NADP+ reductase from Methanococcus vannielii. Biochemistry. 1982 Mar 2;21(5):934–939. doi: 10.1021/bi00534a019. [DOI] [PubMed] [Google Scholar]
  9. Yamazaki S., Tsai L., Stadtman T. C., Jacobson F. S., Walsh C. Stereochemical studies of 8-hydroxy-5-deazaflavin-dependent NADP+ reductase from Methanococcus vannielii. J Biol Chem. 1980 Oct 10;255(19):9025–9027. [PubMed] [Google Scholar]
  10. Zeikus J. G., Fuchs G., Kenealy W., Thauer R. K. Oxidoreductases involved in cell carbon synthesis of Methanobacterium thermoautotrophicum. J Bacteriol. 1977 Nov;132(2):604–613. doi: 10.1128/jb.132.2.604-613.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES