Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

A cytochrome c-550, with mid-point potential +265 mV, has been purified from Thiosphaera pantotropha. The cytochrome was recognised by antibodies to Paracoccus denitrificans cytochrome c-550, but the two proteins were not immunologically identical. Amino acid sequencing of the cytochrome c-550 showed 85.9% and 95.5% identities, respectively, with the cytochromes c-550 of P. denitrificans and Thiobacillus versutus; these are amongst the highest values reported for similarities between class I c-type cytochromes of the c2 group. These similarities are consistent with the published values of 85% for the overall DNA similarity of P. denitrificans and T. pantotropha, but contrast with published 16S rRNA analyses which indicate identity between T. pantotropha and P. denitrificans and 97.5% similarity of T. versutus with these two organisms. Analysis by plasma-desorption mass spectrometry of the peptide containing the haem-binding motif isolated from the apocytochrome has shown that an Hg atom binds to one or both of the two thiol groups.

Original publication

DOI

10.1111/j.1432-1033.1994.tb19974.x

Type

Journal article

Journal

Eur J Biochem

Publication Date

15/01/1994

Volume

219

Pages

585 - 594

Keywords

Amino Acid Sequence, Antibodies, Apoproteins, Chromatography, High Pressure Liquid, Cytochrome c Group, Epitopes, Gram-Negative Chemolithotrophic Bacteria, Macromolecular Substances, Molecular Sequence Data, Molecular Weight, Paracoccus denitrificans, Peptide Fragments, Sequence Homology, Amino Acid, Spectrophotometry