シトクロムb562
WordNet
- (biochemistry) a class of hemoprotein whose principal biological function is electron transfer (especially in cellular respiration)
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English Journal
- Probing Electron Transport in Proteins at Room Temperature with Single-Molecule Precision.
- Inkpen MS, Albrecht T.SourceDepartment of Chemistry, Imperial College London , Exhibition Road, London SW7 2AZ, United Kingdom.
- ACS nano.ACS Nano.2011 Dec 29. [Epub ahead of print]
- Studying electron transport through immobilized proteins at the single-molecule level has been of interest for more than two decades, with a view on the fundamentals of charge transport in condensed media and applications in bioelectronics. Scanning tunneling microscopy (STM) is a powerful tool in t
- PMID 22208640
- Nanosecond Stokes shift dynamics, dynamical transition, and gigantic reorganization energy of hydrated heme proteins.
- Matyushov DV.SourceCenter for Biological Physics, Arizona State University, P.O. Box 871504, Tempe, Arizona 85287-1504, USA. dmitrym@asu.edu
- The journal of physical chemistry. B.J Phys Chem B.2011 Sep 15;115(36):10715-24. Epub 2011 Aug 18.
- We report numerical simulations of three hydrated heme proteins, myoglobin, cytochrome c, and cytochrome B562. The properties of interest are the dynamics and statistics of the electric field and electrostatic potential at heme's iron, as well as their separation into the protein and water component
- PMID 21815677
- The mechanism of superoxide production by the antimycin-inhibited mitochondrial Q-cycle.
- Quinlan CL, Gerencser AA, Treberg JR, Brand MD.SourceBuck Institute for Research on Aging, Novato, California 94945, USA. cquinlan@buckinstitute.org
- The Journal of biological chemistry.J Biol Chem.2011 Sep 9;286(36):31361-72. Epub 2011 Jun 27.
- Superoxide production from antimycin-inhibited complex III in isolated mitochondria first increased to a maximum then decreased as substrate supply was modulated in three different ways. In each case, superoxide production had a similar bell-shaped relationship to the reduction state of cytochrome b
- PMID 21708945
Japanese Journal
- 国際会議レビュー ポスター賞 Construction of Zn-substituted cytochrome b562 assemblies on gold electrode toward efficient photocurrent generation
- 柿倉 泰明
- Bulletin of Japan Society of Coordination Chemistry (57), 88-90, 2011-05
- NAID 40018915891
- Novel Light-Illumination Scanning Tunneling Microscopy Equipped with Optical Fiber Probe
- Nakajima Ken,Lee Bumhwan,Takeda Shuji,Noh Jaegeun,Nagamune Teruyuki,Hara Masahiko
- Japanese journal of applied physics. Pt. 1, Regular papers & short notes 42(7B), 4861-4865, 2003-07-15
- … For this study, self-assembled monolayers (SAMs) of chimera proteins composed of cytochrome $b_{562}$ mutant proteins fused with an enhanced green fluorescent protein (EGFP) were prepared. … With light illumination, the EGFP was excited, resulting in photocurrent generation due to the energy transfer to the cytochrome part instead of a typical fluorescence. …
- NAID 150000041905
- 3R1530 GFP変異体とcytochromeb562のキメラタンパク質への補因子の再構成を用いた人工光合成へ向けた分子設計(28.バイオエンジニアリング,一般講演,日本生物物理学会第40回年会)
Related Links
- Online Macromolecular Musuem ... This protein is mostly alpha helical. It contains 4 amphilphilc helices which are packed other to form a bundle. The helices are antiparallel in that adjacent helices run in opposite directions.
- Abstract We have completed the total chemical synthesis of cytochrome b562 and an axial ligand analogue, [SeMet 7]cyt b562, by thioester-mediated chemical ligation of unprotected peptide ...
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