Upon further analysis, neither cytochrome c554 from Nitrosomonas europaea nor its F156A variant display NO reductase activity, though both proteins bind nitric oxide reversibly-Reference-Cited by-同舟云学术

Upon further analysis, neither cytochrome c554 from Nitrosomonas europaea nor its F156A variant display NO reductase activity, though both proteins bind nitric oxide reversibly

Published:2018-06-26 Issue:6 Volume:23 Page:861-878
ISSN:0949-8257
Container-title:JBIC Journal of Biological Inorganic Chemistry
language:en
Short-container-title:J Biol Inorg Chem

Author:

McGarry Jennifer M.,Pacheco A. Andrew

Funder

National Science Foundation

Publisher

Springer Science and Business Media LLC

Subject

Inorganic Chemistry,Biochemistry

Link

http://link.springer.com/article/10.1007/s00775-018-1582-4/fulltext.html

Reference65 articles.

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2. Iverson TM, Arciero DM, Hsu BT, Logan MSP, Hooper AB, Rees DC (1998) Heme packing motifs revealed by the crystal structure of the tetra-heme cytochrome c554 from Nitrosomonas europaea. Nat Struct Biol 5(11):1005–1012

3. Iverson TM, Arciero DM, Hooper AB, Rees DC (2001) High-resolution structures of the oxidized and reduced states of cytochrome c554 from Nitrosomonas europaea. J Biol Inorg Chem 6(4):390–397

4. Upadhyay AK, Petasis DT, Arciero DM, Hooper AB, Hendrich MP (2003) Spectroscopic characterization and assignment of reduction potentials in the tetraheme cytochrome c(554) from Nitrosomonas europaea. J Am Chem Soc 125(7):1738–1747. https://doi.org/10.1021/Ja020922x

5. Whittaker M, Bergmann D, Arciero D, Hooper AB (2000) Electron transfer during the oxidation of ammonia by the chemolithotrophic bacterium Nitrosomonas europaea. Biochim Biophys Acta Bioenerg 1459(2–3):346–355

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