Literature DB >> 4016136

Characterization of the siroheme active site in spinach nitrite reductase by resonance Raman spectroscopy.

M R Ondrias, S D Carson, M Hirasawa, D B Knaff.   

Abstract

The resonance Raman spectra of various species of spinach nitrite reductase (ferredoxin: nitrite oxidoreductase, EC 1.7.7.1) have been obtained with Soret excitation. These spectra allow for the vibrational properties of the unique siroheme chromophore at the enzyme's active site. The wholesale reordering of siroheme vibrational properties relative to those of protoporphyrins can be rationalized as resulting from a combination of symmetry lowering and bond order reductions within the siroheme macrocyle.

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Year:  1985        PMID: 4016136     DOI: 10.1016/0167-4838(85)90023-8

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  2 in total

1.  A role for cytochrome c and cytochrome c peroxidase in electron shuttling from Erv1.

Authors:  Deepa V Dabir; Edward P Leverich; Sung-Kun Kim; Frederick D Tsai; Masakazu Hirasawa; David B Knaff; Carla M Koehler
Journal:  EMBO J       Date:  2007-11-01       Impact factor: 11.598

2.  The role of tryptophan in the ferredoxin-dependent nitrite reductase of spinach.

Authors:  Jatindra N Tripathy; Masakazu Hirasawa; Sung-Kun Kim; Aaron T Setterdahl; James P Allen; David B Knaff
Journal:  Photosynth Res       Date:  2007-07-05       Impact factor: 3.429

  2 in total

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