共 50 条
Protein Adsorption on Solid Supported Membranes: Monitoring the Transport Activity of P-Type ATPases
被引:7
|作者:
Tadini-Buoninsegni, Francesco
[1
]
机构:
[1] Univ Florence, Dept Chem Ugo Schiff, I-50019 Sesto Fiorentino, Italy
来源:
关键词:
sarcoplasmic reticulum Ca2+-ATPase;
Cu+-ATPase;
phospholipid flippase;
charge displacement;
concentration jump;
solid supported membrane;
conformational transition;
electrogenicity;
ion translocation;
phospholipid flipping;
SARCOPLASMIC-RETICULUM CA-2+-ATPASE;
CRYSTAL-STRUCTURE;
CONFORMATIONAL MEMORY;
CHARGE TRANSLOCATION;
CALCIUM-TRANSPORT;
PUMP ISOFORMS;
CA-ATPASE;
MECHANISM;
COUNTERTRANSPORT;
PHOSPHOLAMBAN;
D O I:
10.3390/molecules25184167
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
P-type ATPases are a large family of membrane transporters that are found in all forms of life. These enzymes couple ATP hydrolysis to the transport of various ions or phospholipids across cellular membranes, thereby generating and maintaining crucial electrochemical potential gradients. P-type ATPases have been studied by a variety of methods that have provided a wealth of information about the structure, function, and regulation of this class of enzymes. Among the many techniques used to investigate P-type ATPases, the electrical method based on solid supported membranes (SSM) was employed to investigate the transport mechanism of various ion pumps. In particular, the SSM method allows the direct measurement of charge movements generated by the ATPase following adsorption of the membrane-bound enzyme on the SSM surface and chemical activation by a substrate concentration jump. This kind of measurement was useful to identify electrogenic partial reactions and localize ion translocation in the reaction cycle of the membrane transporter. In the present review, we discuss how the SSM method has contributed to investigate some key features of the transport mechanism of P-type ATPases, with a special focus on sarcoplasmic reticulum Ca2+-ATPase, mammalian Cu+-ATPases (ATP7A and ATP7B), and phospholipid flippase ATP8A2.
引用
收藏
页数:16
相关论文