By a News Reporter-Staff News Editor at Life Science Weekly -- Research findings on Proteins are discussed in a new report. According to news reporting from Changsha, People's Republic of China, by NewsRx journalists, research stated, "Out-membrane cytochrome c (Cyt c) plays an important role carrying electrons from the inside of microbes to outside electron acceptors. However, the active sites of Cyt c are wrapped by non-conductive peptide chains, hindering direct extracellular electron transfer (EET)."
The news correspondents obtained a quote from the research from Hunan Agricultural University, "Humic acids (HA) have been previously proven to efficiently facilitate EET. However, the inherent mechanism of HA-stimulated BET has not been well interpreted. Here, to probe the mechanism behind HA-stimulated EET, we studied the interaction between Cyt c and HA. The attachment of active in vivo Cyt c on a graphite electrode was achieved when MR-1 cells were self-assembled on the electrode surface. Pure horse-heart Cyt c was covalently immobilized on an electrode via 4-aminobenzoic acid to create an active in vitro Cyt c-enriched surface. Cyclic voltammetic measurements and scanning electron microscopy confirmed the immobilization of bacterial cells and pure Cyt c protein. Electrochemical methods revealed that HA could enhance the electrocatalytic current of both in vitro and in vivo Cyt c towards oxygen and thiosulfate, suggesting enhanced EET. The blue-shifted soret band in the UV-Vis spectra and changes in the excitation/emission matrix fluorescence spectra demonstrated that Cyt c interacted with HA to form organic complexes via electrostatic or hydrogen-bonding interactions."
According to the news reporters, the research concluded: "The results will help understand electron shuttle-stimulated BET and develop bacteria-based bioremediation and bioenergy technologies."
For more information on this research see: Humic acid-enhanced electron transfer of in vivo cytochrome c as revealed by electrochemical and spectroscopic approaches. Journal of Environmental Sciences-China, 2014;26(5):1118-1124. Journal of Environmental Sciences-China can be contacted at: Science Press, 16 Donghuangchenggen North St, Beijing 100717, Peoples R China (see also Proteins).
Our news journalists report that additional information may be obtained by contacting J.H. Tang, Hunan Agr Univ, Coll Biosci & Biotechnol, Changsha 410128, Hunan, People's Republic of China. Additional authors for this research include Y. Liu, Y. Yuan and S.G. Zhou.
Keywords for this news article include: Asia, Changsha, Chemistry, Cytochromes, Hemeproteins, Electrochemical, People's Republic of China
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