The functional role of the structure of the dioxo-isobacteriochlorin in the catalytic site of cytochrome cd1 for the reduction of nitrite

Author:

Fujii Hiroshi12345,Yamaki Daisuke67895,Ogura Takashi101112135,Hada Masahiko67895

Affiliation:

1. Department of Chemistry, Biology and Environmental Science

2. Faculty of Science

3. Nara Women's University

4. Nara 630-8506

5. Japan

6. Department of Chemistry

7. Graduate School of Science

8. Tokyo Metropolitan University

9. Hachioji

10. Department of Life Science and Picobiology Institute

11. Graduate School of Life Science

12. University of Hyogo

13. RSC-UH Leading Program Center

Abstract

We studied the functional role of the unique heme d1 in the catalytic nitrite reduction using synthetic model complexes.

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Reference49 articles.

1. D. Richardson , in Nitrogen Cycling in Bacteria Molecular Analysis, ed. J. W. B. Moir, Caister Academic Press, Norfolk, 2011, pp. 23–37

2. Binding and activation of nitrite and nitric oxide by copper nitrite reductase and corresponding model complexes

3. Nitric Oxide in Biological Denitrification:  Fe/Cu Metalloenzyme and Metal Complex NOx Redox Chemistry

4. W. Schumacher , F.Neese, U.Hole and P. M. H.Kroneck, in Transition Metals in Microbial Metabolism, ed. G. Winkelmann and C. J. Carrano, Harwood Academic Publishers, Amsterdam, 1997, pp. 329–356

5. N-terminal arm exchange is observed in the 2.15 Å crystal structure of oxidized nitrite reductase from Pseudomonas aeruginosa

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