Download Molybdenum Enzymes, Cofactors, and Model Systems PDF Free - Full Version
Download Molybdenum Enzymes, Cofactors, and Model Systems by Edward I. Stiefel, Dimitri Coucouvanis, and William E. Newton (Eds.) in PDF format completely FREE. No registration required, no payment needed. Get instant access to this valuable resource on PDFdrive.to!
About Molybdenum Enzymes, Cofactors, and Model Systems
Content: Molybdenum enzymes, cofactors, and chemistry : an introductory survey / Edward I. Stiefel -- The reaction mechanism of xanthine oxidase / Russ Hille -- Biochemistry of the molybdenum cofactors / K.V. Rajagopalan -- The bacterial molybdenum cofactor / O. Meyer, K. Frunzke, J. Tachil, and M. Volk -- Models of pterin-containing molybdenum enzymes / Charles G. Young and Anthony G. Wedd -- Pterins, quinoxalines, and metallo-ene-dithiolates : synthetic approach to the molybdenum cofactor / Robert S. Pilato, K. Eriksen, M.A. Greaney, Y. Gea, E.C. Taylor, S. Goswami, L. Kilpatrick, T.G. Spiro, A.L. Rheingold, and Edward I. Stiefel -- Strategies for the synthesis of the cofactor of the oxomolybdoenzymes / C.D. Garner, E.M. Armstrong, M.J. Ashcroft, M.S. Austerberry, J.H. Birks, D. Collison, A.J. Goodwin, L. Larsen, D.J. Rowe, and J.R. Russell -- Molybdenum complexes of reduced pterins / Sharon J. Nieter Burgmayer, Kristin Everett, and Laura Bostick -- Chemical and physical coupling of oxomolybdenum centers and iron porphyrins : models for the molybdenum-iron interaction in sulfite oxidase / Michael J. LaBarre, Arnold Raitsimring, and John H. Enemark -- Nitrogenase structure, function, and genetics / Barbara K. Burgess -- Crystal structures of the iron protein and molybdenum-iron protein of nitrogenase / D.C. Rees, J. Kim, M.M. Georgiadis, H. Komiya, A.J. Chirino, D. Woo, J. Schlessman, M.K. Chan, L. Joshua-Tor, G. Santillan, P. Chakrabarti, and B.T. Hsu -- Structure and environment of metal clusters in the nitrogenase molybdenum-iron protein from Clostridium pasteurianum / Jeffrey T. Bolin, Nino Campobasso, Steven W. Muchmore, T. Vance Morgan, and Leonard E. Mortenson -- Biosynthesis of the iron-molybdenum cofactor of nitrogenase / Paul W. Ludden, Vinod K. Shah, Gary P. Roberts, Mary Homer, Ronda Allen, Tim Paustian, Jon Roll, Ranjini Chatterjee, Mark Madden, and Jeff Allen -- Role of the iron-molybdenum cofactor polypeptide environment in Azotobacter vinelandii molybdenum-nitrogenase catalysis / William E. Newton and Dennis R. Dean -- Extended X-ray absorption fine structure and L-edge spectroscopy of nitrogenase molybdenum-iron protein / J. Chen, J. Christiansen, S.J. George, J. van Elp, R. Tittsworth, B.J. Hales, S. Al-Ahmad, Dimitri Coucouvanis, Nino Campobasso, Jeffrey T. Bolin, and S.P. Cramer -- Redox properties of the nitrogenase proteins from Azotobacter vinelandii / G.D. Watt, H. Huang, and K.R.N. Reddy -- The molybdenum-iron protein of nitrogenase : structural and functional features of metal cluster prosthetic groups / W.H. Orme-Johnson -- Protein component complex formation and adenosine triphosphate hydrolysis in nitrogenase / James Bryant Howard -- Electron-transfer reactions associated with nitrogenase from Klebsiella pneumoniae / R.N.F. Thorneley, G.A. Ashby, K. Fisher, and D.J. Lowe -- Recent structure determinations of the molybdenum-iron protein of nitrogenase : impact on design of synthetic analogs for the iron-molybdenum-sulfur active site and the iron-molybdenum cofactor / Dimitri Coucouvanis -- Bonding, activation, and stabilization of small molecules by molybdenum-sulfur and iron-sulfur systems / Dieter Sellmann -- Chemical transformations of coordinated dinitrogen in molybdenum and tungsten phosphine complexes / Masanobu Hidai and Yasushi Mizobe -- Modeling the N-N bond-cleavage step in the reduction of molecular nitrogen to ammonia : protonation and electron-transfer reactions of dinitrogen, nitrogen hydride, and organonitrogen complexes of molybdenum and tungsten / T. Adrian George and Jeffery R.D. DeBord.
Detailed Information
| Author: | Edward I. Stiefel, Dimitri Coucouvanis, and William E. Newton (Eds.) |
|---|---|
| Publication Year: | 1993 |
| Pages: | 390 |
| Language: | English |
| File Size: | 7.953 |
| Format: | |
| Price: | FREE |
Safe & Secure Download - No registration required
Why Choose PDFdrive for Your Free Molybdenum Enzymes, Cofactors, and Model Systems Download?
- 100% Free: No hidden fees or subscriptions required for one book every day.
- No Registration: Immediate access is available without creating accounts for one book every day.
- Safe and Secure: Clean downloads without malware or viruses
- Multiple Formats: PDF, MOBI, Mpub,... optimized for all devices
- Educational Resource: Supporting knowledge sharing and learning
Frequently Asked Questions
Is it really free to download Molybdenum Enzymes, Cofactors, and Model Systems PDF?
Yes, on https://PDFdrive.to you can download Molybdenum Enzymes, Cofactors, and Model Systems by Edward I. Stiefel, Dimitri Coucouvanis, and William E. Newton (Eds.) completely free. We don't require any payment, subscription, or registration to access this PDF file. For 3 books every day.
How can I read Molybdenum Enzymes, Cofactors, and Model Systems on my mobile device?
After downloading Molybdenum Enzymes, Cofactors, and Model Systems PDF, you can open it with any PDF reader app on your phone or tablet. We recommend using Adobe Acrobat Reader, Apple Books, or Google Play Books for the best reading experience.
Is this the full version of Molybdenum Enzymes, Cofactors, and Model Systems?
Yes, this is the complete PDF version of Molybdenum Enzymes, Cofactors, and Model Systems by Edward I. Stiefel, Dimitri Coucouvanis, and William E. Newton (Eds.). You will be able to read the entire content as in the printed version without missing any pages.
Is it legal to download Molybdenum Enzymes, Cofactors, and Model Systems PDF for free?
https://PDFdrive.to provides links to free educational resources available online. We do not store any files on our servers. Please be aware of copyright laws in your country before downloading.
The materials shared are intended for research, educational, and personal use in accordance with fair use principles.
