The structural flexibility of ferric cytochrome c

  title={The structural flexibility of ferric cytochrome c},
  author={Gabriel Otiko and Peter J. Sadler},
  journal={FEBS Letters},
In the eukaryotic mitochondrial respiratory chain, cytochrome c transfers electrons from a reductase complex to cytochrome oxidase, the terminal component which reduces molecular oxygen to water. Cytochrome c is a haem protein containing about 103 amino acids. The haem group is covalently attached to the protein via thioether linkages to one of its edges from Cys 14 and Cys 17, and the iron itself is further coordinated in its fifth and sixth positions to S from Met 80 and N from His 18 [ 11… 
9 Citations
The interaction between cytochrome c and trans-[PtCl2(NH3)2]
The reaction between cytochrome c and trans-[PtCl2(NH3)2] has been studied under different conditions. The complex can not only bind to a Met-80 residue, which causes the Fe–S bond of ferricytochrome
Gold-induced spin-state changes in haem proteins
Abstract During the course of our work on anti-arthritic gold drugs, we discovered that Et3PAuCl converted ferric cytochrome into a novel, green high-spin form at pH 7, ambient temperature [1]. The
Reactions of triethylphosphine gold(I) complexes with heme proteins: novel spin-state changes in cytochrome b562, myoglobin, and hemoglobin.
Two distinct kinetic steps were observed in the autoxidation of HbO2 and MbO2 that may involve the liberation of superoxide and the kinetics of the spin-state change of cyt b562 were too fast to measure by conventional methods.
Phosphines and metal phosphine complexes: Relationship of chemistry to anticancer and other biological activity
Current interest in the biological chemistry of phosphines and their metal complexes ranges from the widespread application of PH3 as a fumigant, to the clinical use of a Au(I)PEt3 complex as an
Effects of gold(I) antiarthritic drugs and related compounds on Pseudomonas putida.
Experiments with 195Au suggested that a mechanism does not exist for the short term uptake of gold by sensitive or resistant bacteria, but the resistant strain appeared to limit gold uptake over a longer term (hours).
Characterization of P—AU—N bonds in the solid state by 15N NMR
The high‐resolution solid‐state and solution 15N NMR spectrum of Et3PAu(phthalimide‐15N) are compared. Both spectra exhibit a remarkably well resolved doublet attributable to the scalar


Photo-oxidative modification of the heme ligands in horse heart ferricytochrome c: conformational and functional studies.
Abstract The selective photo-oxidation of either histidine-18 or methionine-80 of horse heart ferricytochrome c has been achieved. The histidine-18 modified cytochrome exhibits no enzymic activity,
Components of cytochrome c oxidase detectable by EPR spectroscopy.
EPR signals observed with the enzyme between 6 and 100 °K at various states of oxidation and at different conditions of pH and presence of solutes are described in detail and the quantities of paramagnetic species represented by these signals are estimated.
Comparison of the structures of various eukaryotic ferricytochromes c and ferrocytochromes and their antigenic differences.
Differences in structure were shown to correlate with antigenic differences between the various proteins in donkey, cow, dog, rabbit, chicken and pigeon.
Reactions of gold(III) ions with ribonuclease A and methionine derivatives in aqueous solution.
Reactions between model methionine derivatives and Au(III) show that the oxidation involves the production of Au(I)-methionine species, and the stability of these complexes is dependent on the availability of free NH2 groups which catalyse their disproportionation.
Regulation of oxygen affinity of hemoglobin: influence of structure of the globin on the heme iron.
  • M. Perutz
  • Chemistry, Medicine
    Annual review of biochemistry
  • 1979
The heme irons between hemoglobin and myoglobin and physical and chemical Criteria for Quaternary Structure and effects of quaternary structure on thermal spin equilibria are described.
Electronic spectrum of single crystals of ferricytochrome-c.
The absorption spectrum of crystalline horse‐heart ferricytochrome‐c was investigated and the Soret band and main visible band were found to have the same polarization, while the weaker band at 5650 A is polarized differently.
Studies on ferricytochrome c. I. Effect of pH, ionic strength and protein denaturants on the spectra of ferricytochrome c.
Formamide, ethane 1,2-diol and dioxane technical grade, were obtained from Hopkin and Williams Ltd and all solutions were made up using double distilled water.
The biological chemistry of gold: A Metallo-drug and heavy-atom label with variable valency
3. Au ° . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 176 3.1. Na tu ra l Up take . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
SK&F 36914--an agent for oral chrysotherapy.
Oral administration of chlorine (triethylphosphine) gold (SK&F 36914) produced lower gold levels in both serum and kidneys than equivalent therapeutic doses of parenteral gold sodium thiomalate, and would appear to have potential as an agent for oral chrysotherapy.