scholarly journals Direct electron transfer-type bioelectrocatalysis by membrane-bound aldehyde dehydrogenase from Gluconobacter oxydans and cyanide effects on its bioelectrocatalytic properties

2020 ◽  
pp. 106911
Author(s):  
Taiki Adachi ◽  
Yuki Kitazumi ◽  
Osamu Shirai ◽  
Kenji Kano
Keyword(s):  
Electron Transfer ◽  
Aldehyde Dehydrogenase ◽  
Direct Electron Transfer ◽  
Gluconobacter Oxydans ◽  
Membrane Bound

scholarly journals Oriented Immobilization of a Membrane-Bound Hydrogenase onto an Electrode for Direct Electron Transfer

Langmuir ◽  
2011 ◽  
Vol 27 (10) ◽  
pp. 6449-6457 ◽  
Author(s):  
Cristina Gutiérrez-Sánchez ◽  
David Olea ◽  
Marta Marques ◽  
Victor M. Fernández ◽  
Inês A. C. Pereira ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Direct Electron Transfer ◽  
Oriented Immobilization ◽  
Membrane Bound

scholarly journals X-ray structure of the direct electron transfer-type FAD glucose dehydrogenase catalytic subunit complexed with a hitchhiker protein

2019 ◽  
Vol 75 (9) ◽  
pp. 841-851 ◽  
Author(s):  
Hiromi Yoshida ◽  
Katsuhiro Kojima ◽  
Masaki Shiota ◽  
Keiichi Yoshimatsu ◽  
Tomohiko Yamazaki ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Disulfide Bonds ◽  
Hydrophobic Interactions ◽  
Direct Electron Transfer ◽  
Glucose Dehydrogenase ◽  
Catalytic Subunit ◽  
Effective Electron ◽  
Α Subunit ◽  
X Ray ◽  
Membrane Bound

The bacterial flavin adenine dinucleotide (FAD)-dependent glucose dehydrogenase complex derived from Burkholderia cepacia (BcGDH) is a representative molecule of direct electron transfer-type FAD-dependent dehydrogenase complexes. In this study, the X-ray structure of BcGDHγα, the catalytic subunit (α-subunit) of BcGDH complexed with a hitchhiker protein (γ-subunit), was determined. The most prominent feature of this enzyme is the presence of the 3Fe–4S cluster, which is located at the surface of the catalytic subunit and functions in intramolecular and intermolecular electron transfer from FAD to the electron-transfer subunit. The structure of the complex revealed that these two molecules are connected through disulfide bonds and hydrophobic interactions, and that the formation of disulfide bonds is required to stabilize the catalytic subunit. The structure of the complex revealed the putative position of the electron-transfer subunit. A comparison of the structures of BcGDHγα and membrane-bound fumarate reductases suggested that the whole BcGDH complex, which also includes the membrane-bound β-subunit containing three heme c moieties, may form a similar overall structure to fumarate reductases, thus accomplishing effective electron transfer.

scholarly journals An electron transfer competent structural ensemble of membrane-bound cytochrome P450 1A1 and cytochrome P450 oxidoreductase

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Goutam Mukherjee ◽  
Prajwal P. Nandekar ◽  
Rebecca C. Wade
Keyword(s):  
Electron Transfer ◽  
Cytochrome P450 ◽  
Drug Targets ◽  
Catalytic Domain ◽  
Cytochrome P450 1A1 ◽  
P450 Oxidoreductase ◽  
Distal Side ◽  
Cytochrome P450 Oxidoreductase ◽  
Membrane Bound ◽  
Transient Interactions

AbstractCytochrome P450 (CYP) heme monooxygenases require two electrons for their catalytic cycle. For mammalian microsomal CYPs, key enzymes for xenobiotic metabolism and steroidogenesis and important drug targets and biocatalysts, the electrons are transferred by NADPH-cytochrome P450 oxidoreductase (CPR). No structure of a mammalian CYP–CPR complex has been solved experimentally, hindering understanding of the determinants of electron transfer (ET), which is often rate-limiting for CYP reactions. Here, we investigated the interactions between membrane-bound CYP 1A1, an antitumor drug target, and CPR by a multiresolution computational approach. We find that upon binding to CPR, the CYP 1A1 catalytic domain becomes less embedded in the membrane and reorients, indicating that CPR may affect ligand passage to the CYP active site. Despite the constraints imposed by membrane binding, we identify several arrangements of CPR around CYP 1A1 that are compatible with ET. In the complexes, the interactions of the CPR FMN domain with the proximal side of CYP 1A1 are supplemented by more transient interactions of the CPR NADP domain with the distal side of CYP 1A1. Computed ET rates and pathways agree well with available experimental data and suggest why the CYP–CPR ET rates are low compared to those of soluble bacterial CYPs.

scholarly journals Amperometric Biosensors Based on Direct Electron Transfer Enzymes

Molecules ◽  
2021 ◽  
Vol 26 (15) ◽  
pp. 4525
Author(s):  
Franziska Schachinger ◽  
Hucheng Chang ◽  
Stefan Scheiblbrandner ◽  
Roland Ludwig
Keyword(s):  
Electron Transfer ◽  
Electrode Materials ◽  
Direct Electron Transfer ◽  
Accurate Determination ◽  
Direct Electrochemistry ◽  
Product Analysis ◽  
Amperometric Biosensors ◽  
Chemical Surface ◽  
Fusion Enzymes ◽  
Cost Efficient

The accurate determination of analyte concentrations with selective, fast, and robust methods is the key for process control, product analysis, environmental compliance, and medical applications. Enzyme-based biosensors meet these requirements to a high degree and can be operated with simple, cost efficient, and easy to use devices. This review focuses on enzymes capable of direct electron transfer (DET) to electrodes and also the electrode materials which can enable or enhance the DET type bioelectrocatalysis. It presents amperometric biosensors for the quantification of important medical, technical, and environmental analytes and it carves out the requirements for enzymes and electrode materials in DET-based third generation biosensors. This review critically surveys enzymes and biosensors for which DET has been reported. Single- or multi-cofactor enzymes featuring copper centers, hemes, FAD, FMN, or PQQ as prosthetic groups as well as fusion enzymes are presented. Nanomaterials, nanostructured electrodes, chemical surface modifications, and protein immobilization strategies are reviewed for their ability to support direct electrochemistry of enzymes. The combination of both biosensor elements—enzymes and electrodes—is evaluated by comparison of substrate specificity, current density, sensitivity, and the range of detection.

scholarly journals Enhancement of Direct Electron Transfer in Graphene Bioelectrodes Containing Novel Cytochrome c Variants with Optimized Heme Orientation

2021 ◽  
pp. 107818
Author(s):  
Miriam Izzo ◽  
Silvio Osella ◽  
Margot Jacquet ◽  
Małgorzata Kiliszek ◽  
Ersan Harputlu ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Direct Electron Transfer
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