Results 31 to 40 of about 292,332 (117)

Cj1411c encodes for a cytochrome P450 involved in Campylobacter jejuni 81-176 pathogenicity. [PDF]

open access: yesPLoS ONE, 2013
Cytochrome P450s are b-heme-containing enzymes that are able to introduce oxygen atoms into a wide variety of organic substrates. They are extremely widespread in nature having diverse functions at both biochemical and physiological level.
Luis A J Alvarez   +6 more
doaj   +1 more source

Electricity Generation by Shewanella decolorationis S12 without Cytochrome c

open access: yesFrontiers in Microbiology, 2017
Bacterial extracellular electron transfer (EET) plays a key role in various natural and engineering processes. Outer membrane c-type cytochromes (OMCs) are considered to be essential in bacterial EET.
Yonggang Yang   +6 more
doaj   +1 more source

The cryoEM structure of cytochrome bd from C. glutamicum provides novel insights into structural properties of actinobacterial terminal oxidases

open access: yesFrontiers in Chemistry, 2023
Cytochromes bd are essential for microaerobic respiration of many prokaryotes including a number of human pathogens. These enzymes catalyze the reduction of molecular oxygen to water using quinols as electron donors.
Tamara N. Grund   +9 more
doaj   +1 more source

Effect of pH on the thermostability and redox properties of cytochrome c552 from Wolinella succinogenes

open access: yesFrontiers in Chemical Biology
Cytochrome c552 from Wolinella succinogenes is one of the few examples of a low reduction potential class I c-type cytochrome with a mixture of high/low spin state populations observed in its visible spectrum.
Vitor H. Mordido   +10 more
doaj   +1 more source

A Membrane-Bound Cytochrome Enables Methanosarcina acetivorans To Conserve Energy from Extracellular Electron Transfer

open access: yesmBio, 2019
Extracellular electron exchange in Methanosarcina species and closely related Archaea plays an important role in the global carbon cycle and enhances the speed and stability of anaerobic digestion by facilitating efficient syntrophic interactions.
Dawn E. Holmes   +6 more
doaj   +1 more source

Effects of pH on kinetics of the structural rearrangement that gates the electron-transfer reaction between zinc cytochrome c and plastocyanin. Analysis of protonation states in a diprotein complex [PDF]

open access: yesJournal of the Serbian Chemical Society, 2003
Electron transfer from zinc cytochrome c to copper(II)plastocyanin in the electrostatically-stabilized complex [Crnogorac MM, Shen C, Young S, Hansson O, Kosti} NM (1996) Biochemistry 35, 16465–74].
NENAD M. KOSTIC, MILAN M. CRNOGORAC
doaj   +3 more sources

K-shell Analysis Reveals Distinct Functional Parts in an Electron Transfer Network and Its Implications for Extracellular Electron Transfer

open access: yesFrontiers in Microbiology, 2016
Shewanella oneidensis MR-1 is capable of extracellular electron transfer (EET) and hence has attracted considerable attention. The EET pathways mainly consist of c-type cytochromes, along with some other proteins involved in electron transfer processes ...
Dewu eDing   +3 more
doaj   +1 more source

Development and validation of the method for determination of encapsulation efficiency of cytochrome c in liposomes

open access: yesФармацевтичний журнал, 2018
A strategic pathway in creating high-potent medical products is with targeted therapeutic systems that are based on nanoparticles of various structure.
O. G. Katsai   +3 more
doaj   +1 more source

Conformational Change of Wild Type Cytochrome c Characterized by NMR Spectroscopy at Natural Isotropic Abundance

open access: yesChinese Journal of Magnetic Resonance, 2019
Cytochrome c is an important multifunctional protein, which plays important roles in the respiratory chain and cell apoptosis. Characterization of conformational changes of cytochrome c is essential to elucidate the molecular mechanism underlying its ...
FANG Zhong-pei   +5 more
doaj   +1 more source

Widespread Distribution and Functional Specificity of the Copper Importer CcoA: Distinct Cu Uptake Routes for Bacterial Cytochrome c Oxidases

open access: yesmBio, 2018
Cytochrome c oxidases are members of the heme-copper oxidase superfamily. These enzymes have different subunits, cofactors, and primary electron acceptors, yet they all contain identical heme-copper (CuB) binuclear centers within their catalytic subunits.
Bahia Khalfaoui-Hassani   +7 more
doaj   +1 more source

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