کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8298797 | 1537045 | 2013 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Molecular basis of [FeFe]-hydrogenase function
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کلمات کلیدی
ADTCPIDDHHYSCOREHyperfine sublevel correlation spectroscopyDFT - DFT[FeFe]-hydrogenase - [FeFe] هیدروژنازGreen algae - جلبک سبزOxygen sensitivity - حساسیت اکسیژنMolecular dynamics - دینامیک ملکولی یا پویایی مولکولیFerredoxin - فریدوکسیینMolecular mechanics - مکانیک مولکولیQuantum mechanics - مکانیک کوانتومDensity functional theory - نظریه تابعی چگالیClostridium - کلوستریدیوم
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The precise electrochemical features of metal cofactors that convey the functions of redox enzymes are essentially determined by the specific interaction pattern between cofactor and enclosing protein environment. However, while biophysical techniques allow a detailed understanding of the features characterizing the cofactor itself, knowledge about the contribution of the protein part is much harder to obtain. [FeFe]-hydrogenases are an interesting class of enzymes that catalyze both, H2 oxidation and the reduction of protons to molecular hydrogen with significant efficiency. The active site of these proteins consists of an unusual prosthetic group (H-cluster) with six iron and six sulfur atoms. While H-cluster architecture and catalytic states during the different steps of H2 turnover have been thoroughly investigated during the last 20Â years, possible functional contributions from the polypeptide framework were only assumed according to the level of conservancy and X-ray structure analyses. Due to the recent development of simpler and more efficient expression systems the role of single amino acids can now be experimentally investigated. This article summarizes, compares and categorizes the results of recent investigations based on site directed and random mutagenesis according to their informative value about structure function relationships in [FeFe]-hydrogenases. This article is part of a Special Issue entitled: Metals in Bioenergetics and Biomimetics Systems.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1827, Issues 8â9, AugustâSeptember 2013, Pages 974-985
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1827, Issues 8â9, AugustâSeptember 2013, Pages 974-985
نویسندگان
Martin Winkler, Julian Esselborn, Thomas Happe,