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pro vyhledávání: '"J. Baz Jackson"'
Autor:
J. Baz Jackson
Publikováno v:
Life, Vol 7, Iss 3, p 36 (2017)
We have recently criticised the natural pH gradient hypothesis which purports to explain how the difference in pH between fluid issuing from ancient alkali vents and the more acidic Hadean ocean could have driven molecular machines that catalyse reac
Externí odkaz:
https://doaj.org/article/bd7b05659de14a6585bdfbe88eb96c25
Autor:
J. Baz Jackson
Publikováno v:
Journal of Molecular Evolution. 85:1-7
It has been suggested that inorganic membranes were forerunners of organic membranes at the origin of life. Such membranes, interposed between alkaline fluid in submarine vents and the more acidic Hadean ocean, were thought to house inorganic molecul
Publikováno v:
FEBS Letters. 589:2027-2033
The membrane protein transhydrogenase in animal mitochondria and bacteria couples reduction of NADP+ by NADH to proton translocation. Recent X-ray data on Thermus thermophilus transhydrogenase indicate a significant difference in the orientations of
Autor:
J. Baz Jackson
Publikováno v:
Journal of Molecular Evolution
The hypothesis that a natural pH gradient across inorganic membranes lying between the ocean and fluid issuing from hydrothermal alkali vents provided energy to drive chemical reactions during the origin of life has an attractive parallel with chemio
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1807(1):85-94
In its forward direction, transhydrogenase couples the reduction of NADP + by NADH to the outward translocation of protons across the membrane of bacteria and animal mitochondria. The enzyme has three components: dI and dIII protrude from the membran
Autor:
Lisa Giachini, Federico Boscherini, J. Baz Jackson, Giovanni Venturoli, Francesco Francia, Giulia Veronesi, Nick P.J. Cotton, Simon J. Whitehead
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1797:494-500
Transhydrogenase couples hydride transfer between NADH and NADP(+) to proton translocation across a membrane. The binding of Zn(2+) to the enzyme was shown previously to inhibit steps associated with proton transfer. Using Zn K-edge X-ray absorption
Autor:
J. Baz Jackson, Tina Bhakta, Timothy R. Dafforn, Simon J. Whitehead, Scott A. White, John Wilkie, John S. Snaith, Sundaresan Rajesh
Publikováno v:
Biochemistry. 46:3304-3318
Transhydrogenase couples the redox reaction between NADH and NADP+ to proton translocation across a membrane. The enzyme comprises three components; dI binds NAD(H), dIII binds NADP(H), and dII spans the membrane. The 1,4,5,6-tetrahydro analogue of N
Publikováno v:
Biochemistry. 43:10952-10964
Transhydrogenase couples the redox (hydride-transfer) reaction between NAD(H) and NADP(H) to proton translocation across a membrane. The redox reaction is catalyzed at the interface between two components (dI and dIII) which protrude from the membran
Publikováno v:
Biochemistry. 42:1217-1226
Transhydrogenase, found in bacterial membranes and inner mitochondrial membranes of animal cells, couples the redox reaction between NAD(H) and NADP(H) to proton translocation. In this work, the invariant Gln132 in the NAD(H)-binding component (dI) o
Publikováno v:
Biochemistry. 41:4173-4185