Cytochrome c-553 from Desulfovibrio vulgaris exhibits a highly exposed heme and an
unusually low reduction potential with respect to other c-type cytochromes. Solvent heme …

Cytochrome c 6A is a unique dithio-cytochrome of green algae and plants. It has a very
similar core structure to that of bacterial and algal cytochromes c 6, but is unable to fulfil the …

Cytochromes are involved in a wide variety of redox reactions in living systems. Some of
them contain multiple hemes such as Desulfovibrio cytochrome c 3 and Shewanella small …

This is a thorough biochemical, spectroscopic, electrochemical, and structural study of a
cytochrome c 6 isolated from the filamentous green alga Cladophora glomerata. The protein …

The cytochrome (cyt) c 1 heme of the ubihydroquinone: cytochrome c oxidoreductase (bc 1
complex) is covalently attached to two cysteine residues of the cyt c 1 polypeptide chain via …

Cytochromes c 3 isolated from Desulfovibrio spp. are periplasmic proteins that play a central
role in energy transduction by coupling the transfer of electrons and protons from …

The 20-kDa di-heme cytochrome c 4 from the psycrophilic bacterium Pseudoalteromonas
haloplanktis TAC 125 was cloned and expressed in Escherichia coli and investigated …

The first three-dimensional structure of a dimeric, octa-heme cytochrome c 3 (M r 26000)
from Desulfovibrio desulfuricans Norway, established at 2.2 Å resolution, is briefly presented …

Cytochrome c 6A is a unique dithio-cytochrome of green algae and plants. It has a very
similar core structure to that of bacterial and algal cytochromes c 6 but is unable to fulfill the …

Cytochrome c 3 (M r 26000) isolated from Desulfovibrio gigas is a dimeric cytochrome
consisting of two identical subunits of 109 amino acids, each of which contains four haem …