Structural role of the tyrosine residues of cytochrome c [PDF]
, 1982 The tertiary structures of horse, tuna, Neurospora crassa, horse [Hse65,Leu67]- and horse [Hse65,Leu74]-cytochromes c were studied with high-resolution 1H n.m.r. spectroscopy.
Boon, Peter J. +7 more
core
Semisynthetic cytochrome c. [PDF]
Proceedings of the National Academy of Sciences, 1977 Horse heart cytochrome c can be split with cyanogen bromide into a heme peptide (residues 1-65) and a nonheme peptide (residues 66-104). In a process involving (i) complex formation between the two fragments and (ii) restoration of the severed peptide linkage, a fully active cytochrome c preparation can be re-formed.
Leon E. Barstow +6 more
openaire +3 more sources
The role of biotransformation processes in mediating interactions between psychotropic drugs and natural products [PDF]
, 2020 Many patients are not aware that natural products such as fruit juices or plant infusions can cause significant interactions with several drugs, some of which can be dangerous, especially when the medical treatment is for neurological or psychiatric ...
Bacinschi, Nicolae +6 more
core +1 more source
Cytochromes c of Campylobacter sputorum subspecies mucosalis [PDF]
, 1982 Campylobacter sputorum subspecies mucosalis, the causative organism of porcine intestinal adenomatosis, will grow microaerophillically in the presence of hydrogen as an electron donor, and under these conditions contains a high complement of c-type ...
Elkurdi, A.B.
core
Ultrastructure and biochemical function of the mitochondria in respiratory-deficient mutant yeast induced by 4-nitroquinoline nitrogen oxide [PDF]
, 1969 1. A respiratory-deficient mutant strain of yeast was obtained from wild strain of Saccharomyces servisiae by treatment with 4-nitroquinoline N-oxide. Ultrastructure and function of the wild or mutant strains and the mitochondrial fractions isolated from
Goto, Nobuyuki +3 more
core +1 more source
The pio Operon Is Essential for Phototrophic Fe(II) Oxidation in Rhodopseudomonas palustris TIE-1 [PDF]
, 2006 Phototrophic Fe(II)-oxidizing bacteria couple the oxidation of ferrous iron [Fe(II)] to reductive CO2 fixation by using light energy, but until recently, little has been understood about the molecular basis for this process. Here we report the discovery,
Jiao, Yongqin, Newman, Dianne K.
core +4 more sources
Characterisation of MtoD from Sideroxydans lithotrophicus: a cytochrome c electron shuttle used in lithoautotrophic growth [PDF]
, 2015 The autotrophic Sideroxydans lithotrophicus ES-1 can grow by coupling the oxidation of ferrous iron to the reduction of oxygen. Soluble ferrous iron is oxidised at the surface of the cell by an MtoAB porin-cytochrome complex that functions as an electron
Beckwith, Chris +6 more
core +2 more sources
Thermodynamic Volume Cycles for Electron Transfer in the Cytochrome c Oxidase and for the Binding of Cytochrome c to Cytochrome c Oxidase [PDF]
Biophysical Journal, 1998 Dilatometry is a sensitive technique for measuring volume changes occurring during a chemical reaction. We applied it to the reduction-oxidation cycle of cytochrome c oxidase, and to the binding of cytochrome c to the oxidase. We measured the volume changes that occur during the interconversion of oxidase intermediates.
Gaston Hui Bon Hoa +4 more
openaire +3 more sources
Successive translocation into and out of the mitochondrial matrix [PDF]
, 1987 We investigated the import and sorting pathways of cytochrome b2 and cytochrome c1, which are functionally located in the intermembrane space of mitochondria.
Alt +67 more
core +1 more source
Evolution of the Couple Cytochrome c and Cytochrome c Oxidase in Primates [PDF]
, 2012 Mitochondrial energy metabolism has been affected by a broad set of ancient and recent evolutionary events. The oldest example is the endosymbiosis theory that led to mitochondria and a recently proposed example is adaptation to cold climate by anatomically modern human lineages.
Denis Pierron +4 more
openaire +3 more sources