Bis-Methionine Ligation to Heme Iron in Mutants of Cytochrome b562. 2. Characterization by NMR of Heme−Ligand Interactions
Author:
Affiliation:
1. Centre for Protein Engineering, MRC Centre, Hills Road, Cambridge CB2 2QH, U.K., and MRC Unit for Protein Function and Design, University Chemical Laboratory, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K.
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi961128p
Reference39 articles.
1. pH-Linked conformational regulation of a metalloprotein oxidation-reduction equilibrium: electrochemical analysis of the alkaline form of cytochrome c
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1. Metalloprotein Design and Engineering;Encyclopedia of Inorganic and Bioinorganic Chemistry;2014-06-16
2. Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers;Chemical Reviews;2014-04-23
3. Thiol, Disulfide, and Trisulfide Complexes of Ru Porphyrins: Potential Models for Iron–Sulfur Bonds in Heme Proteins;Journal of the American Chemical Society;2012-02-06
4. Metalloprotein Design & Engineering;Encyclopedia of Inorganic and Bioinorganic Chemistry;2011-12-15
5. Characterization of SiaA, a Streptococcal Heme-Binding Protein Associated with a Heme ABC Transport System;Biochemistry;2008-02-01
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