The solution structure of reduced Bacillus pasteurii cytochrome c, which has only 71 amino acids, has been determined by NMR to an RMSD of 0.46 +/- 0.08 Angstrom for all backbone atoms and 0.79 +/- 0.08 Angstrom for all heavy atoms and refined through restrained energy minimization. The target function out of 1645 constraints is 0.52 +/- 0.11 Angstrom(2), and the penalty function is 66 12 kJ mol(-1). The structure appears very similar to that in the oxidized state, only Trp87 and the propionates showing significant differences. The mobility was investigated through N-15 R-1 and R-2 relaxation rates, N-15-H-1 NOE, and H-1/H-2 exchange. It is found that the oxidized form is generally more mobile than the reduced one. By comparing the redox-state dependence of the structural/dynamic properties of Fe-S proteins, cytochrome c, and blue copper proteins, hints are provided for a better comprehension of the electron transfer processes.

Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processes / BARTALESI I.; I. BERTINI; ROSATO A.. - In: BIOCHEMISTRY. - ISSN 0006-2960. - STAMPA. - 42:(2003), pp. 739-745. [10.1021/bi0266028]

Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processes

BERTINI, IVANO;ROSATO, ANTONIO
2003

Abstract

The solution structure of reduced Bacillus pasteurii cytochrome c, which has only 71 amino acids, has been determined by NMR to an RMSD of 0.46 +/- 0.08 Angstrom for all backbone atoms and 0.79 +/- 0.08 Angstrom for all heavy atoms and refined through restrained energy minimization. The target function out of 1645 constraints is 0.52 +/- 0.11 Angstrom(2), and the penalty function is 66 12 kJ mol(-1). The structure appears very similar to that in the oxidized state, only Trp87 and the propionates showing significant differences. The mobility was investigated through N-15 R-1 and R-2 relaxation rates, N-15-H-1 NOE, and H-1/H-2 exchange. It is found that the oxidized form is generally more mobile than the reduced one. By comparing the redox-state dependence of the structural/dynamic properties of Fe-S proteins, cytochrome c, and blue copper proteins, hints are provided for a better comprehension of the electron transfer processes.
2003
42
739
745
BARTALESI I.; I. BERTINI; ROSATO A.
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/202940
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