Chapter 4 The Neurospora crassa plasma membrane H+ -ATPase

作者: Gene A. Scarborough

DOI: 10.1016/S0167-7306(08)60066-6

关键词:

摘要: Publisher Summary This chapter discusses the structure and dynamics of Neurospora ATPase other P-type ATPases, allowing formulation an approximate structural model for these enzymes. It information available on catalytic mechanism H + -ATPase enzymes within framework this model. From considerations, relatively straightforward schemes molecular mechanisms by which ATPases might catalyze ATP hydrolysis-driven ion translocation can be visualized. Progress toward understanding any enzyme usually depends ease with isolated, amounts obtainable, stability final preparation. The gene sequence indicates presence eight cysteine residues in molecule. To ascertain chemical state residues, direct studies established cystine reagents have been carried out. Titrations reagent—dithiobisnitrobenzoate—and reagent—nitrothiosulfobenzoate—indicated six free cysteines one disulfide bridge

参考文章(94)
RAMÓN SERRANO, Plasma membrane ATPase of fungi and plants as a novel type of proton pump Current Topics in Cellular Regulation. ,vol. 23, pp. 87- 126 ,(1984) , 10.1016/B978-0-12-152823-2.50007-6
TerrenceL. Scott, Molecular topography of the Ca2+-ATPase of sarcoplasmic reticulum. Molecular and Cellular Biochemistry. ,vol. 82, pp. 51- 54 ,(1988) , 10.1007/BF00242515
LINUS PAULING, Molecular Architecture and Biological Reactions Chemical & Engineering News. ,vol. 24, pp. 1375- 1377 ,(1946) , 10.1021/CEN-V024N010.P1375
G A Scarborough, R Addison, On the subunit composition of the Neurospora plasma membrane H+-ATPase. Journal of Biological Chemistry. ,vol. 259, pp. 9109- 9114 ,(1984) , 10.1016/S0021-9258(17)47272-3
W P Jencks, How does a calcium pump pump calcium? Journal of Biological Chemistry. ,vol. 264, pp. 18855- 18858 ,(1989) , 10.1016/S0021-9258(19)47232-3