Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

sup 1 H NMR spectra of vertebrate (2Fe-2S) ferredoxins. Hyperfine resonances suggest different electron delocalization patterns from plant ferredoxins

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00101a024· OSTI ID:5821852
;  [1]; ;  [2]
  1. Univ. of Wisconsin, Madison (United States)
  2. Univ. of California, Irvine (United States)

The authors report the observation of paramagnetically shifted (hyperfine) proton resonances from vertebrate mitochondrial (2Fe-2S) ferredoxins. The hyperfine signals of human, bovine, and chick (2Fe-2S) ferredoxins are described and compared with those of Anabena 7120 vegetative ferredoxin, a plant-type (2Fe-2S) ferredoxin studied previously. The hyperfine resonances of the three vertebrate ferredoxins were very similar to one another both in the oxidized state and in the reduced state, and slow (on the NMR scale) electron self-exchange was observed in partially reduced samples. For the oxidized vertebrate ferredoxins, hyperfine signals were observed downfield of the diamagnetic envelope from +13 to +50 ppm, and the general pattern of peaks and their anti-Curie temperature dependence are similar to those observed for the oxidized plant-type ferredoxins. For the reduced vertebrate ferredoxins, hyperfine signals were observed for the oxidized plant-type ferredoxins. For the reduced vertebrate ferredoxins, hyperfine signals were observed both upfield ({minus}2 to {minus}18 ppm) and downfield (+15 to +45 ppm), and all were found to exhibit Curie-type temperature dependence. These results indicate that the contact-shifted resonances in the reduced vertebrate ferredoxins detect different spin magnetization from those in the reduced plant ferredoxins and suggest that plant and vertebrate ferredoxins have fundamentally different patterns of electron delocalization in the reduced (2Fe-2S) center.

OSTI ID:
5821852
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 30:37; ISSN 0006-2960; ISSN BICHA
Country of Publication:
United States
Language:
English