LDR | | 01893nmm uu200421 4500 |
001 | | 000000334623 |
005 | | 20240805180700 |
008 | | 181129s2018 |||||||||||||||||c||eng d |
020 | |
▼a 9780355969009 |
035 | |
▼a (MiAaPQ)AAI10602526 |
035 | |
▼a (MiAaPQ)ucdavis:17161 |
040 | |
▼a MiAaPQ
▼c MiAaPQ
▼d 248032 |
082 | 0 |
▼a 574 |
100 | 1 |
▼a Pham, Cindy C. |
245 | 10 |
▼a Spectroscopic Investigations of [FeFe]-Hydrogenases - Catalysis and Maturation. |
260 | |
▼a [S.l.] :
▼b University of California, Davis.,
▼c 2018 |
260 | 1 |
▼a Ann Arbor :
▼b ProQuest Dissertations & Theses,
▼c 2018 |
300 | |
▼a 338 p. |
500 | |
▼a Source: Dissertation Abstracts International, Volume: 79-09(E), Section: B. |
500 | |
▼a Adviser: Stephen P. Cramer. |
502 | 1 |
▼a Thesis (Ph.D.)--University of California, Davis, 2018. |
506 | |
▼a This item is not available from ProQuest Dissertations & Theses. |
520 | |
▼a [FeFe]-hydrogenase (FeFe-H2ase) is a prime candidate for alternative hydrogen energy producers. FeFe-H2ase catalyzes the inter-conversion of H2 into electrons and protons. The active site of the enzyme contains [4Fe4S] cluster and [2Fe2S]-subclu |
520 | |
▼a To help elucidate the catalytic mechanism of this facinating enzyme, we investigated the resting states and trapped intermediate of the active site using NRVS. Selective labeling of catalytic intermediates of FeFe-H2ase makes NRVS ideal for anal |
590 | |
▼a School code: 0029. |
650 | 4 |
▼a Biochemistry. |
650 | 4 |
▼a Physical chemistry. |
690 | |
▼a 0487 |
690 | |
▼a 0494 |
710 | 20 |
▼a University of California, Davis.
▼b Chemistry. |
773 | 0 |
▼t Dissertation Abstracts International
▼g 79-09B(E). |
773 | |
▼t Dissertation Abstract International |
790 | |
▼a 0029 |
791 | |
▼a Ph.D. |
792 | |
▼a 2018 |
793 | |
▼a English |
856 | 40 |
▼u http://www.riss.kr/pdu/ddodLink.do?id=T14996616
▼n KERIS |
980 | |
▼a 201812
▼f 2019 |
990 | |
▼a 관리자 |