A two-dimensional 1H-NMR study on Megasphaera elsdenii flavodoxin in the oxidized state and some comparisons with the two-electron-reduced state.
Assignments for the 137 amino acid residues of oxidized Megasphaera elsdenii flavodoxin have been made using the sequential resonance assignment procedure. Great benefit was experienced from assignments of the fully reduced protein. The secondary and tertiary structures of the typical alpha/beta protein remain virtually identical on going from the oxidized to the two-electron-reduced state as judged from two-dimensional NOE spectroscopy. However, functionally important conformation changes in the flavin-binding region do occur on reduction. Considerable reduction-state-dependent chemical shift variations of protons in the immediate vicinity of the isoalloxazine moiety take place. From analysis of these shifts, it can be concluded that ring current effects of the pyrazine part of the flavin diminish on two-electron reduction.
van Mierlo
C P
CP
Department of Biochemistry, Agricultural University, Wageningen, The Netherlands.
van der Sanden
B P
BP
van Woensel
P
P
Müller
F
F
Vervoort
J
J
D000595:Amino Acid Sequence; D001665:Binding Sites; D005486:Flavin Mononucleotide / Q000378:metabolism; D005418:Flavodoxin / Q000378:metabolism / Q000648:ultrastructure*; D006873:Hydroquinones; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011809:Quinones; D045854:Veillonellaceae / Q000032:analysis*
D005418:Flavodoxin; D006873:Hydroquinones; D011809:Quinones; D005486:Flavin Mononucleotide