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J Biol Chem, Vol. 274, Issue 53, 38032-38041, December 31, 1999

Definition of the Interaction Domain for Cytochrome c on Cytochrome c Oxidase
I. BIOCHEMICAL, SPECTRAL, AND KINETIC CHARACTERIZATION OF SURFACE MUTANTS IN SUBUNIT II OF RHODOBACTER SPHAEROIDES CYTOCHROME aa₃^*

Yuejun Zhen, Curtis W. Hoganson^§, Gerald T. Babcock^§, and Shelagh Ferguson-Miller^¶

From the Departments of  Biochemistry and ^§ Chemistry, Michigan State University, East Lansing, Michigan 48824

To determine the interaction site for cytochrome c (Cc) on cytochrome c oxidase (CcO), a number of conserved carboxyl residues in subunit II of Rhodobacter sphaeroides CcO were mutated to neutral forms. A highly conserved tryptophan, Trp¹⁴³, was also mutated to phenylalanine and alanine. Spectroscopic and metal analyses of the surface carboxyl mutants revealed no overall structural changes. The double mutants D188Q/E189N and D151Q/E152N exhibit similar steady-state kinetic behavior as wild-type oxidase with horse Cc and R. sphaeroides Cc₂, showing that these residues are not involved in Cc binding. The single mutants E148Q, E157Q, D195N, and D214N have decreased activities and increased K_m values, indicating they contribute to the Cc:CcO interface. However, their reactions with horse and R. sphaeroides Cc are different, as expected from the different distribution of surface lysines on these cytochromes c. Mutations at Trp¹⁴³ severely inhibit activity without changing the K_m for Cc or disturbing the adjacent Cu_A center. From these data, we identify a Cc binding area on CcO with Trp¹⁴³ and Asp²¹⁴ close to the site of electron transfer and Glu¹⁴⁸, Glu¹⁵⁷, and Asp¹⁹⁵ providing electrostatic guidance. The results are completely consistent with time-resolved kinetic measurements (Wang, K., Zhen, Y., Sadoski, R., Grinnell, S., Geren, L., Ferguson-Miller, S., Durham, B., and Millett, F. (1999) J. Biol. Chem. 274, 38042-38050) and computational docking analysis (Roberts, V. A., and Pique, M. E. (1999) J. Biol. Chem. 274, 38051-38060).

This paper is dedicated to Emmanuel Margoliash in honor of his 80th birthday and four decades of exceptional contributions to the understanding of cytochrome c.

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