MARC details
| 000 -LEADER |
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02605nam a2200241Ia 4500 |
| 003 - CONTROL NUMBER IDENTIFIER |
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MX-MdCICY |
| 005 - DATE AND TIME OF LATEST TRANSACTION |
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| control field |
20250625124716.0 |
| 040 ## - CATALOGING SOURCE |
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| Transcribing agency |
CICY |
| 090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN) |
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| Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) |
B-8220 |
| 008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION |
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250602s9999 xx |||||s2 |||| ||und|d |
| 245 10 - TITLE STATEMENT |
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| Title |
Heterologous expression and properties of the Q-subunit of the Fe-only hydrogenase from Thermotoga maritima |
| 490 0# - SERIES STATEMENT |
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| Volume/sequential designation |
Biochimica et Biophysica Acta, 1505(2-3), p.209-219, 2001 |
| 520 3# - SUMMARY, ETC. |
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| Summary, etc. |
Thermotoga maritima is a hyperthermophilic bacterium that contains a complex, heterotrimeric (KLQ)Fe-only hydrogenase. Sequence analysis indicates that the gene encoding the smallest subunit (Q), hydC, contains a predicted ironsulfur cluster binding motif. However, characterization of the native Q-subunit has been hampered by interference from and the inability to separate intact Q-subunit from the other two subunits (K and L). To investigate the function and properties of the isolated Q-subunit, the gene encoding HydG was expressed in Escherichia coli. Two forms of the recombinant protein were obtained with molecular masses of 10 and 18 kDa, respectively. Both contained a single [2Fe-2S]cluster based on metal analysis, EPR and UV-visible spectroscopy. NH2-terminal sequencing revealed that the 10 kDa protein is a truncated form of the intact Q-subunit and lacks the first 65 amino acid residues. The midpoint potential of the 18 kDa form was 3356 mV at pH 7.0 and 25³C, as measured by direct electrochemistry, and was pH dependent with a pKox of 7.5 and a pKred of 7.7. The oxidized, recombinant Q-subunit was stable at 80³C under anaerobic conditions with a half-life greater than 24 h, as judged by the UV-visible spectrum of the [2Fe-2S]cluster. In the presence of air the protein was less stable and denatured with a halflife of approx. 2.5 h. The recombinant Q-subunit was electron transfer competent and was efficiently reduced by pyruvate ferredoxin oxidoreductase from Pyrococcus furiosus, with a Km of 5 WMand a Vmax of 9 U/mg. In contrast, native T. maritima hydrogenase holoenzyme and its separated K-subunit were much less effective electron donors for the Q-subunit, with a Vmax of 0.01 U/mg and 0.1 U/mg, respectively |
| 650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM |
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| Topical term or geographic name entry element |
THERMOTOGA MARITIMA HYDC |
| 650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM |
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| Topical term or geographic name entry element |
FE-ONLY HYDROGENASE |
| 650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM |
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| Topical term or geographic name entry element |
HETEROLOGOUS GENE EXPRESSION |
| 700 12 - ADDED ENTRY--PERSONAL NAME |
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| Personal name |
Verhagen, M.F.J.M. |
| 700 12 - ADDED ENTRY--PERSONAL NAME |
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| Personal name |
O'Rourke, T.W. |
| 700 12 - ADDED ENTRY--PERSONAL NAME |
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| Personal name |
Lal Menon, A. |
| 700 12 - ADDED ENTRY--PERSONAL NAME |
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| Personal name |
Adams, M.W.W. |
| 856 40 - ELECTRONIC LOCATION AND ACCESS |
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| Uniform Resource Identifier |
<a href="https://drive.google.com/file/d/1yXJ1ll5vIlB212UipC510xT9GpFK4hv5/view?usp=drivesdk">https://drive.google.com/file/d/1yXJ1ll5vIlB212UipC510xT9GpFK4hv5/view?usp=drivesdk</a> |
| Public note |
Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx |
| 942 ## - ADDED ENTRY ELEMENTS (KOHA) |
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| Source of classification or shelving scheme |
Clasificación local |
| Koha item type |
Documentos solicitados |
