Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Zhi H. Zhou"'
Autor:
Yuan Sun, Xiao Y. Tang, Yang Bai, Yu Q. Chen, Zhi H. Zhou, Rui T. Wu, Yao Y. Zheng, Jiao L. Wu, Tian Lan, Jing-Yun Ma
Publikováno v:
SSRN Electronic Journal.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1b5726e62a60e566660012c23d9eca71
https://doi.org/10.2139/ssrn.4041013
https://doi.org/10.2139/ssrn.4041013
Publikováno v:
European Journal of Biochemistry. 266:1158-1165
Thermococcus litoralis is a hyperthermophilic archaeon that grows at temperatures up to 98 °C by fermentative metabolism and reduces elemental sulfur (S0) to H2S. A [NiFe] hydrogenase, responsible for H2S or H2 production, has been purified and char
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4a5b7f8e0571036cccdd83e3b909f8f4
https://doi.org/10.1046/j.1432-1327.1999.00969.x
https://doi.org/10.1046/j.1432-1327.1999.00969.x
Publikováno v:
Biochemistry. 37:7351-7362
The ferredoxin (7.5 kDa) of the hyperthermophilic archaeon, Pyrococcus furiosus, contains a single [4Fe-4S]1+,2+ cluster that is coordinated by three Cys and one Asp residue rather than the expected four Cys. The role of this Asp residue was investig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56d39c04ff83fd958b56e254707b5f1d
https://doi.org/10.1021/bi972864b
https://doi.org/10.1021/bi972864b
Publikováno v:
Biochemistry. 37:3377-3385
As part of our studies on the structural and dynamic properties of hyperthermostable proteins, we have investigated the unfolding pathways of the small iron−sulfur protein rubredoxin from Pyrococcus furiosus (RdPf) at pH 2. Unfolding has been initi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6733661475d69cc3031a68989542e3a3
https://doi.org/10.1021/bi9721804
https://doi.org/10.1021/bi9721804
Publikováno v:
Biochemistry. 34:7161-7169
The hyperthermophilic bacterium Thermotoga maritima and the hyperthermophilic archaeon Pyrococcus furiosus grow optimally at 80 and 100 degrees C, respectively, by the fermentation of carbohydrates to organic acids, CO2, and H2. Pyruvate is a major s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1aaa23287c9260a4d8f9253481c3b76a
https://doi.org/10.1021/bi00021a030
https://doi.org/10.1021/bi00021a030
Publikováno v:
Biochemistry. 37(10)
The temperature dependence of the unfolding kinetics of rubredoxins from the hyperthermophile Pyrococcus furiosus (RdPf) and the mesophile Clostridium pasteurianum (RdCp) has been studied. Results show that RdPf unfolds much more slowly, under all ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c103f4c46f51757cba7c956036b9f6f0
https://pubmed.ncbi.nlm.nih.gov/9521657
https://pubmed.ncbi.nlm.nih.gov/9521657
Autor:
Zhi H. Zhou, Michael W. W. Adams, Roberto P. Christen, Eugene T. Smith, John M. Tomich, Tatyana Jancic
Publikováno v:
Journal of inorganic biochemistry. 65(1)
The entire polypeptide of hyperthermophilic Pyrococcus furiosus rubredoxin was synthesized in order to specifically probe structural determinants of protein thermostability. The uv-visible, circular dichroic, electron paramagnetic, and nuclear magnet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce66d3ba189c4281126b0ebb794ce5ed
https://pubmed.ncbi.nlm.nih.gov/8987170
https://pubmed.ncbi.nlm.nih.gov/8987170
Publikováno v:
Biochemistry. 34(31)
The bases of the hyperthermostability of rubredoxin from Pyrococcus furiosus (RdPf) have been probed by structural perturbations induced by solution pH and ionic strength changes. Comparison of the solution behavior at pH 7 and pH 2, as probed by far
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b17154b305266f05c0e3338de9aeb34
https://pubmed.ncbi.nlm.nih.gov/7632687
https://pubmed.ncbi.nlm.nih.gov/7632687
Publikováno v:
Biochemistry. 31(47)
The 3Fe forms of ferredoxins (Fd) from the hyperthermophilic archaebacteria Pyrococcus furiosus (Pf) and Thermococcus litoralis (Tl) have been investigated by 1H NMR. A combination of one-dimensional nuclear Overhauser and two-dimensional NOESY and b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5aacd2d91388aa6c312a699b8ea7b697
https://pubmed.ncbi.nlm.nih.gov/1445925
https://pubmed.ncbi.nlm.nih.gov/1445925
Autor:
Zhi H. Zhou, Craig D. Adams, S. Nomikos, John M. Tomich, Eugene T. Smith, Michael W. W. Adams, H. Chapman
Publikováno v:
Journal of Inorganic Biochemistry. 59:575
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f3e8dde1f7147b1e6f50c002634d6d48
https://doi.org/10.1016/0162-0134(95)97670-l
https://doi.org/10.1016/0162-0134(95)97670-l