Experimental evidence of an alpha helix in Desulfovibrio desulfuricans Norway ferredoxin I: a two-dimensional NMR study

D Marion; F Guerlesquin

doi:10.1016/0006-291x(89)90035-1

Experimental evidence of an alpha helix in Desulfovibrio desulfuricans Norway ferredoxin I: a two-dimensional NMR study

Biochem Biophys Res Commun. 1989 Mar 15;159(2):592-8. doi: 10.1016/0006-291x(89)90035-1.

Authors

D Marion¹, F Guerlesquin

Affiliation

¹ Laboratory of Chemical Physics, N.I.D.D.K., Bethesda, MD 20892.

PMID: 2930532
DOI: 10.1016/0006-291x(89)90035-1

Abstract

Desulfovibrio ferredoxins are small proteins involved in biological oxido-reduction reactions and contain either one or two (4Fe-4S) clusters. The conformation of D. desulfuricans Norway ferredoxin I in solution was studied by two-dimensional NMR and various conformational parameters (n.O.e. and J-coupling) indicate the presence of an alpha-helix involving residues 41 to 50. These data confirm an earlier proposal (Fukuyama et al, J. Mol. Biol. 199, 183 (1988] in which the space of the missing cluster in monocluster ferredoxins is occupied by an alpha-helix. The evolutionary relevance of this result is discussed in view of published sequences and structures of related ferredoxins.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Amino Acid Sequence
Desulfovibrio / analysis*
Ferredoxins*
Magnetic Resonance Spectroscopy* / methods
Molecular Sequence Data
Protein Conformation
Sequence Homology, Nucleic Acid

Substances

Ferredoxins