Abstract
The H+-translocating ATP synthase functioning on the plasma membrane of Halobacterium halobium is found to be different from F0F1-ATPase/synthase which has been believed to be ubiquitous as the proton-motive ATP synthase in all respiring organisms on our biosphere.
The synthase includes the 320 kDa component possibly as the catalytic part (ATPase when released from the membrane) which is composed of two pairs of 86 kDa and 64 kDa subunits, and the 78 kDa (and/or 12 kDa) subunit possibly as the membrane/anchor part.
This work was supported partly by Grant-in-Aid for Scientific Research on Priority Areas of “Bioenergetics” to Y.M. from the Ministry of Education, Sscience and Culture, Japan.
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© 1989 Plenum Press, New York
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Mukohata, Y. et al. (1989). A H+-Translocating ATP Synthase in an Extremely Halophilic Archaebacterium. In: Marzuki, S. (eds) Molecular Structure, Function, and Assembly of the ATP Synthases. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0593-4_15
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DOI: https://doi.org/10.1007/978-1-4613-0593-4_15
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