Related Experiment Video
Updated: Aug 11, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Specific cation binding site in mammalian cytochrome oxidase
A Kirichenko1, T Vygodina, H M Mkrtchyan
1A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia.
Abstract:
Calcium ion binds reversibly with cytochrome c oxidase from beef heart mitochondria (Kd approximately 2 microM) shifting alpha- and gamma-absorption bands of heme a to the red. Two sodium ions compete with one Ca2+ for the binding site with an average dissociation constant square root[K1(Na) x K2(Na)] approximately 3.6 mM. The Ca2+-induced spectral shift of heme a is specific for mammalian cytochrome c oxidase and is not observed in bacterial or yeast aa3 oxidases although the Ca2+-binding site has been revealed in the bacterial enzyme [Ostermeier, C., Harrenga, A., Ermler, U. and Michel, H. (1997) Proc. Natl. Acad. Sci. USA 94, 10547-10553]. As His-59 and Gln-63 involved in Ca2+ binding with Subunit I of P. denitrificans oxidase are not conserved in bovine oxidase, these residues have to be substituted by alternative ligands in mammalian enzyme, which is indeed the case as shown by refined structure of bovine heart cytochrome oxidase (S. Yoshikawa, personal communication). We propose that it is interaction of Ca2+ with the species-specific ligand(s) in bovine oxidase that accounts for perturbation of heme a. The Ca2+/Na2+-binding site may be functionally associated with the exit part of 'pore B' proton channel in subunit I of mammalian cytochrome c oxidase.
More Related Videos
11:04Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
Published on: September 7, 2019
12:26Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability
Published on: June 2, 2023
Related Concept Videos
Ligand Binding Sites
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Ligand Binding and Linkage
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Electron Transport Chain: Complex III and IV