Homotropic and heterotropic cooperativity in the tetrahaem cytochrome c3 from Desulfovibrio vulgaris

This publication has 12 references indexed in Scilit:

• Isolation and Characterization of Flavoredoxin, a New Flavoprotein That Permits in Vitro Reconstitution of an Electron Transfer Chain from Molecular Hydrogen to Sulfite Reduction in the Bacterium Desulfovibrio gigas
  Archives of Biochemistry and Biophysics, 1993
• Assignment of heme resonances in the 1H NMR spectrum of oxidized Desulfovibrio vulgaris (Hildenborough) cytochrome c3
  Inorganica Chimica Acta, 1992
• Assignment of the redox potentials to the four haems in Desulfovibrio vulgaris cytochrome c₃ by 2D‐NMR
  FEBS Letters, 1992
• Involvement of a labile axial histidine in coupling electron and proton transfer in Methylophilus methylotrophus cytochrome c″
  European Journal of Biochemistry, 1992
• A thermodynamic model for the cooperative functional properties of the tetraheme cytochrome c₃ from Desulfovibrio gigas
  European Journal of Biochemistry, 1991
• Full assignment of heme redox potentials of cytochrome c₃ of D. vulgaris Miyazaki F by ¹H‐NMR
  FEBS Letters, 1991
• Estimation of microscopic redox potentials of a tetraheme protein, cytochrome c3 of Desulfovibrio vulgaris, Miyazaki F and partial assignments of heme groups
  Biochemistry, 1990
• NMR studies of electron transfer mechanisms in a protein with interacting redox centres: Desulfovibrio gigas cytochrome c₃
  European Journal of Biochemistry, 1984
• Outline structure of cytochrome c3 and consideration of its properties
  Nature, 1974
• Phosphorylation coupled with electron transfer in extracts of the sulfate reducing bacterium, Desulfovibriogigas
  Biochemical and Biophysical Research Communications, 1966