Buch-Pedersen M J, Palmgren M G
Department of Plant Biology, Royal Veterinary and Agricultural University, Thorvaldsensvej 40, opg. 8, 5 sal, 1871 Frederiksberg, Denmark.
J Plant Res. 2003 Dec;116(6):507-15. doi: 10.1007/s10265-003-0111-9. Epub 2003 Aug 13.
The mechanism of proton translocation by P-type proton ATPases is poorly defined. Asp684 in transmembrane segment M6 of the Arabidopsis thaliana AHA2 plasma membrane P-type proton pump is suggested to act as an essential proton acceptor during proton translocation. Arg655 in transmembrane segment M5 seems to be involved in this proton translocation too, but in contrast to Asp684, is not essential for transport. Asp684 may participate in defining the E(1) proton-binding site, which could possibly exist as a hydronium ion coordination center. A model of proton translocation of AHA2 involving the side chains of amino acids Asp684 and Arg655 is discussed.
P型质子ATP酶质子转运的机制尚不清楚。拟南芥AHA2质膜P型质子泵跨膜片段M6中的天冬氨酸684被认为在质子转运过程中作为必需的质子受体。跨膜片段M5中的精氨酸655似乎也参与了这种质子转运,但与天冬氨酸684不同,它对转运不是必需的。天冬氨酸684可能参与定义E(1)质子结合位点,该位点可能作为水合氢离子配位中心存在。讨论了一个涉及天冬氨酸684和精氨酸655侧链的AHA2质子转运模型。