An analysis of pseudocontact shifts and their relationship to structural features of the redox states of cytochrome b5
- 3 September 1990
- journal article
- Published by Wiley in FEBS Letters
- Vol. 269 (2) , 297-304
- https://doi.org/10.1016/0014-5793(90)81180-v
Abstract
The assignment of proton resonances inboth redox states of a heme protein is necessary for the evaluation of pseudocontact shift data. Many new assignments are presented here for cytochrome b 5 particularly in the paramagnetic oxidised state, thereby allowing both the calculation of electronic g‐tensor values with the magnetic axis orientation and a comparison of observed and calculated pseudocontact shifts utilising a computational procedure. The possible redox linked confonnational changes are found to be minimal in contrast with cytochrome c although the procedure additionally highlights aspects of the mobility of certain residues in cytochrome b 5. In this respect the residue Gly‐42 appears mobile both by this method and by the observation from NMR spectra of a major and minor conformation in this region.Keywords
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