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~~ ~ Cells from oxygen-limi ted cultures of Acetobacter pasteurianus NCIB 6428 contained cyto- chrome d, a 596 nm absorbance (in reduced minus oxidized difference spectra at room temperature) similar to cytochrome a,, and b-type cytochromes, including a cytochrome o-like pigment. Oxygen-sufficient cells lacked the d and a,-like components. Pyridine haemochrome spectra suggested the presence of haem a. Photolysis with white light at - 126 "C of an anoxic suspension of reduced oxygen-limited cells, into which CO had been bubbled, elicited a photodissociation spectrum that revealed the cytochrome o-like species, but not cytochromes d or a,. When a similar suspension, but to which O2 had been added at - 23 "C, was photolysed at - 126 to - 132 "C, using white light or irradiation with a He-Ne laser, an additional, intense absorbance at 648 nm (relative to the CO-Iiganded, reduced form) was observed, attributable to an oxygenated (Fe2+02 or Fe3+O:) complex of cytochrome oxidase d. Photolysis at progressively warmer temperatures, or successive scans of a sample photolysed at -91 "C, revealed (i) increasing depth of a trough (relative to the CO-liganded, reduced form) at 598 nm attributed to the a,-like haemoprotein and (ii) cytochrome b oxidation. Laser photolysis of the cytochrome d-CO complex at - 8 1 "C in the presence of oxygen suggested that oxidation of cytochrome a, preceded that of cytochrome(s) b. It is proposed that, in this strain of Acetobacter, a cytochrome a, -like pigment mediates electron transfer from cytochrome(s) b to cytochrome oxidase d, but that cytochrome a, is not itself an oxidase.

microbiology

The Cytochromes of Acetobacter pasteurianus NCIB 6428. Evidence of a Role for a Cytochrome a1-like Haemoprotein in Electron Transfer to Cytochrome Oxidase d