Applications of B3LYP Method for Enzyme Reactions: O[sub 2] Reduction by Cytochrome c Oxidase and Ubiquinol Oxidation by Cytochrome bc[sub 1] Complex

2007 ◽  
Author(s):  
Yasunori Yoshioka ◽  
George Maroulis ◽  
Theodore E. Simos
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Enzyme Reactions ◽  
Cytochrome Bc ◽  
B3lyp Method

From B to A: making an essential cofactor in a human parasite

2017 ◽  
Vol 474 (18) ◽  
pp. 3089-3092
Author(s):  
Naomi S. Morrissette ◽  
Celia W. Goulding
Keyword(s):  
Cytochrome C ◽  
Trypanosoma Cruzi ◽  
Cytochrome C Oxidase ◽  
Human Disease ◽  
Recent Issue ◽  
Enzyme Reactions ◽  
Human Parasite ◽  
Biochemical Journal ◽  
Eukaryotic Organisms ◽  
Subsequent Activity

Trypanosomatids are parasitic eukaryotic organisms that cause human disease. These organisms have complex lifestyles; cycling between vertebrate and insect hosts and alternating between two morphologies; a replicating form and an infective, nonreplicating one. Because trypanosomatids are one of the few organisms that do not synthesize the essential cofactor, heme, these parasites sequester the most common form, heme B, from their hosts. Once acquired, the parasites derivatize heme B to heme A by two sequential enzyme reactions. Although heme C is found in many cytochrome c and c1 proteins, heme A is the cofactor of only one known protein, cytochrome c oxidase (CcO). In a recent issue of the Biochemical Journal, Merli et al. [Biochem. J. (2017) 474, 2315–2332] demonstrate that the final step in the synthesis of heme A by heme A synthase (TcCox15) and the subsequent activity of CcO are essential for infectivity and replication of Trypanosoma cruzi.

scholarly journals The Yeast Aac2 Protein Exists in Physical Association with the Cytochromebc1-COX Supercomplex and the TIM23 Machinery

2008 ◽  
Vol 19 (9) ◽  
pp. 3934-3943 ◽  
Author(s):  
Mary K. Dienhart ◽  
Rosemary A. Stuart
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Affinity Purification ◽  
Yeast Saccharomyces Cerevisiae ◽  
Present Evidence ◽  
Cytochrome Bc ◽  
Saccharomyces Cerevisiae Mitochondria ◽  
Mitochondrial Inner Membrane ◽  
Physical Association

The ADP/ATP carrier (AAC) proteins play a central role in cellular metabolism as they facilitate the exchange of ADP and ATP across the mitochondrial inner membrane. We present evidence here that in yeast (Saccharomyces cerevisiae) mitochondria the abundant Aac2 isoform exists in physical association with the cytochrome c reductase (cytochrome bc1)-cytochrome c oxidase (COX) supercomplex and its associated TIM23 machinery. Using a His-tagged Aac2 derivative and affinity purification studies, we also demonstrate here that the Aac2 isoform can be affinity-purified with other AAC proteins. Copurification of the Aac2 protein with the TIM23 machinery can occur independently of its association with the fully assembled cytochrome bc1-COX supercomplex. In the absence of the Aac2 protein, the assembly of the cytochrome bc1-COX supercomplex is perturbed, whereby a decrease in the III2-IV2assembly state relative to the III2-IV form is observed. We propose that the association of the Aac2 protein with the cytochrome bc1-COX supercomplex is important for the function of the OXPHOS complexes and for the assembly of the COX complex. The physiological implications of the association of AAC with the cytochrome bc1-COX-TIM23 supercomplex are also discussed.

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