Heme-Heme Orientation and Electron Transfer Kinetic Behavior of Multisite Oxidation-Reduction Enzymes

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Abstract
Analysis of the polarized single-crystal absorption spectra of cytochrome cd 1 of Pseudomonas aeruginosa shows that the heme c and heme d 1 groups in each subunit are oriented perpendicularly to each other in both oxidized and reduced forms of the enzyme. These results, together with those of previous kinetic studies, indicate that a perpendicular heme-heme orientation may be an important factor in specifying kinetically slow steps in a sequential series of electron transfer reactions.