Literature DB >> 6628687

Resolution of the hemes of hydroxylamine oxidoreductase by redox potentiometry and optical spectroscopy.

R C Prince, C Larroque, A B Hooper.   

Abstract

Optical spectroscopy combined with redox potentiometry has resolved the hemes of hydroxylamine oxidoreductase into 6 thermodynamically distinct classes. There are apparently 4 classes of heme c553, with Em7-values of 295 mV, 10 mV, -190 mV and -390 mV, present in a stoichiometry of 1:1:2:1; two equivalents of heme c559, Em7 O mV, and one of heme P-460, an unusual chromophore, with Em7 -260 mV.

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Year:  1983        PMID: 6628687     DOI: 10.1016/0014-5793(83)81154-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  Isolation of a multiheme protein with features of a hydrazine-oxidizing enzyme from an anaerobic ammonium-oxidizing enrichment culture.

Authors:  Munetaka Shimamura; Takashi Nishiyama; Hiroyuki Shigetomo; Takeshi Toyomoto; Yuka Kawahara; Kenji Furukawa; Takao Fujii
Journal:  Appl Environ Microbiol       Date:  2006-12-15       Impact factor: 4.792

Review 2.  Multi-heme proteins: nature's electronic multi-purpose tool.

Authors:  Kathryn D Bewley; Katie E Ellis; Mackenzie A Firer-Sherwood; Sean J Elliott
Journal:  Biochim Biophys Acta       Date:  2013-04-02
  2 in total

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