F e-only hydrogenases: structure, function and evolution (Record no. 42556)
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| 000 -LEADER | |
|---|---|
| fixed length control field | 01995nam a2200193Ia 4500 |
| 003 - CONTROL NUMBER IDENTIFIER | |
| control field | MX-MdCICY |
| 005 - DATE AND TIME OF LATEST TRANSACTION | |
| control field | 20250625124716.0 |
| 040 ## - CATALOGING SOURCE | |
| Transcribing agency | CICY |
| 090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN) | |
| Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) | B-8250 |
| 008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION | |
| fixed length control field | 250602s9999 xx |||||s2 |||| ||und|d |
| 245 10 - TITLE STATEMENT | |
| Title | F e-only hydrogenases: structure, function and evolution |
| 490 0# - SERIES STATEMENT | |
| Volume/sequential designation | Journal of Inorganic BioChemistry, 91(1), p.1-8, 2002 |
| 520 3# - SUMMARY, ETC. | |
| Summary, etc. | Hydrogenases are enzymes capable of catalyzing the oxidation of molecular hydrogen or its production from protons and electrons 1 2 according to the reversible reaction: H á2H 12e . Most of these enzymes fall into to major classes: NiFe and Fe-only hydrogenases. 2 Extensive spectroscopic, electrochemical and structural studies have shed appreciable light on the catalytic mechanism of hydrogenases. Although evolutionarily unrelated, NiFe and Fe-hydrogenases share a common, unusual feature: an active site low-spin Fe center with CO and CN coordination. We have recently focused our attention on Fe-hydrogenases because from structural studies by us and others, it appears to be a simpler system than the NiFe counterpart. Thus the primary hydrogen binding site has been identified and plausible, electron, proton and hydrogen pathways from and to the buried active site may be proposed from the structural data. The extensive genome sequencing effort currently under way has shown that eukaryotic organisms contain putatively gene coding sequences that display significant homology to Fe-hydrogenases. Here, we summarize the available evidence concerning the mechanism of these enzymes and carry out a structural comparison between Fe-hydrogenases and related proteins of unknown metal content from yeast, plant, worm, insect and mammals. |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Nicolet, Y. |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Cavazza, C. |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Fontecilla-Camps, J.C. |
| 856 40 - ELECTRONIC LOCATION AND ACCESS | |
| Uniform Resource Identifier | <a href="https://drive.google.com/file/d/1Ze827VbYU4S99_TgMNnlNzYJda9uE2Pa/view?usp=drivesdk">https://drive.google.com/file/d/1Ze827VbYU4S99_TgMNnlNzYJda9uE2Pa/view?usp=drivesdk</a> |
| Public note | Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx |
| 942 ## - ADDED ENTRY ELEMENTS (KOHA) | |
| Source of classification or shelving scheme | Clasificación local |
| Koha item type | Documentos solicitados |
| Lost status | Source of classification or shelving scheme | Damaged status | Not for loan | Collection | Home library | Current library | Shelving location | Date acquired | Total checkouts | Full call number | Date last seen | Price effective from | Koha item type |
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| Clasificación local | Ref1 | CICY | CICY | Documento préstamo interbibliotecario | 25.06.2025 | B-8250 | 25.06.2025 | 25.06.2025 | Documentos solicitados |