Effect of metronidazole (MNZ) treatment (oral and ip) on activities of cytochrome b5 and P-450 was studied in male, virgin and pregnant female mice. Activities of both the cytochromes increased in virgin mice treated with 2 mg (ip or PO, per mouse) but not in male and pregnant females. 30 mg dose (per mouse) was toxic in pregnant mice but increased the cytochromes activities in males and virgin...

Examining electron transfer between two proteins with identical spectroscopic signatures is a challenging task. It is supposed that several multiheme cytochromes in Shewanella oneidensis form a molecular "wire" through which electrons are transported across the cellular space and a direct study of this transient protein-protein interaction has not yet been reported. In this study, we present va...

The cytochromes c are a family of hemoproteins that share a number of structural features: a thioether linkage between the protein and the heme, histidine and methionine as the fifth and sixth iron ligands, and a tertiary structure known as the "cytochrome fold." These proteins follow a common mechanism of equilibrium unfolding in methanol and acid, differing only in their reactivity to the den...

Beef heart cytochrome c oxidase contains two cytochromes, a and a3, and Pseudomonas aeruginosa cytochrome c peroxidase has one high- and one low-potential c haem, cHP and cLP. The parallelism in co-ordination and spin states between cytochrome a and haem cHP on the one hand and between cytochrome a3 and haem cLP on the other is illustrated. The two latter haems become accessible to cyanide, whe...

Cytochromes c are electron transfer proteins containing one or more hemes covalently bound to the polypeptide chain. Not only are they widely used as models to address a number of issues (including electron transfer, apoptosis and protein folding) but they are also of interest in terms of development of expression protocols for proteins containing posttranslationally attached prosthetic groups....

The polychlorinated biphenyl mixture, Aroclor 1254, is a powerful inducer of both cytochromes P-450 and P-448 exhibiting the catalytic properties of both cytochromes in the liver. Addition of Aroclor 1254 to hepatic microsomes produces a type I difference spectrum. When administered to rats, the hemeprotein induced by Aroclor 1254 displayed spectral properties which are a combination of the spe...

A detailed spectrophotometric study was made of the electron transport systems in .mitochondria from wild type and poky strains of Neurospora crassa. Wild type mitochondria were found to contain flavoproteins, two b-type cytochromes (G-peaks (77%) at 554 and 561 nm), two c-type cytochromes (a-peaks (77°K) at 545 and 550 nm), and cytochrome (1~73 (a-peak (77°K) at 601 nm). In terms of their spec...

The Rhodobacter capsulatus cbb(3)-type cytochrome c oxidase (cbb(3)-Cox) belongs to the heme-copper oxidase superfamily, and its subunits are encoded by the ccoNOQP operon. Biosynthesis of this enzyme is complex and needs dedicated biogenesis genes (ccoGHIS). It also relies on the c-type cytochrome maturation (Ccm) process, which requires the ccmABCDEFGHI genes, because two of the cbb(3)-Cox su...

The major soluble c-type cytochromes in cultured cells of Bradyrhizobium japonicum USDA 110 comprised a CO-reactive c555 (Mr, approximately 15,500) and a non-CO-reactive c550 (Mr, approximately 12,500). Levels of cytochrome per gram of soluble protein in aerobic, anaerobic, and symbiotic cells were 32, 21, and 30 nmol, respectively, for c555 and 31, 44, and 65 nmol, respectively, for c550. The ...