scholarly journals Cytochrome b5 reductase–cytochrome b5 as an active P450 redox enzyme system in Phanerochaete chrysosporium: Atypical properties and in vivo evidence of electron transfer capability to CYP63A2

2011 ◽  
Vol 509 (1) ◽  
pp. 26-32 ◽  
Author(s):  
Khajamohiddin Syed ◽  
Chandramohan Kattamuri ◽  
Thomas B. Thompson ◽  
Jagjit S. Yadav
Keyword(s):  
Electron Transfer ◽  
Phanerochaete Chrysosporium ◽  
Enzyme System ◽  
Cytochrome B5 ◽  
Redox Enzyme ◽  
Cytochrome B5 Reductase ◽  
Transfer Capability

Contribution of Electrostatics to the Kinetics of Electron Transfer from NADH-Cytochrome b5 Reductase to Fe(III)-Cytochrome b5

2016 ◽  
Vol 120 (33) ◽  
pp. 8193-8207 ◽  
Author(s):  
Sireesha Kollipara ◽  
Shivakishore Tatireddy ◽  
Thusitha Pathirathne ◽  
Lasantha K. Rathnayake ◽  
Scott H. Northrup
Keyword(s):  
Electron Transfer ◽  
Cytochrome B5 ◽  
Cytochrome B5 Reductase ◽  
Nadh Cytochrome ◽  
Kinetics Of

scholarly journals Defining the Role of the NADH-Cytochrome-b5 Reductase 3 in the Mitochondrial Amidoxime Reducing Component Enzyme System

2016 ◽  
Vol 44 (10) ◽  
pp. 1617-1621 ◽  
Author(s):  
B. Plitzko ◽  
A. Havemeyer ◽  
B. Bork ◽  
F. Bittner ◽  
R. Mendel ◽  
...  
Keyword(s):  
Enzyme System ◽  
Cytochrome B5 ◽  
Cytochrome B5 Reductase ◽  
Nadh Cytochrome

scholarly journals Structural Features of Cytochrome b5–Cytochrome b5 Reductase Complex Formation and Implications for the Intramolecular Dynamics of Cytochrome b5 Reductase

2021 ◽  
Vol 23 (1) ◽  
pp. 118
Author(s):  
Carlos Gutiérrez-Merino ◽  
Oscar H. Martínez-Costa ◽  
Maria Monsalve ◽  
Alejandro K. Samhan-Arias
Keyword(s):  
Electron Transfer ◽  
Conformational Changes ◽  
Computational Analysis ◽  
Catalytic Domain ◽  
Cytochrome B5 ◽  
Protein Structures ◽  
Reactive Oxygen ◽  
Electron Acceptors ◽  
Functional Sites ◽  
Cytochrome B5 Reductase

Membrane cytochrome b5 reductase is a pleiotropic oxidoreductase that uses primarily soluble reduced nicotinamide adenine dinucleotide (NADH) as an electron donor to reduce multiple biological acceptors localized in cellular membranes. Some of the biological acceptors of the reductase and coupled redox proteins might eventually transfer electrons to oxygen to form reactive oxygen species. Additionally, an inefficient electron transfer to redox acceptors can lead to electron uncoupling and superoxide anion formation by the reductase. Many efforts have been made to characterize the involved catalytic domains in the electron transfer from the reduced flavoprotein to its electron acceptors, such as cytochrome b5, through a detailed description of the flavin and NADH-binding sites. This information might help to understand better the processes and modifications involved in reactive oxygen formation by the cytochrome b5 reductase. Nevertheless, more than half a century since this enzyme was first purified, the one-electron transfer process toward potential electron acceptors of the reductase is still only partially understood. New advances in computational analysis of protein structures allow predicting the intramolecular protein dynamics, identifying potential functional sites, or evaluating the effects of microenvironment changes in protein structure and dynamics. We applied this approach to characterize further the roles of amino acid domains within cytochrome b5 reductase structure, part of the catalytic domain, and several sensors and structural domains involved in the interactions with cytochrome b5 and other electron acceptors. The computational analysis results allowed us to rationalize some of the available spectroscopic data regarding ligand-induced conformational changes leading to an increase in the flavin adenine dinucleotide (FAD) solvent-exposed surface, which has been previously correlated with the formation of complexes with electron acceptors.

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