Reply to Pancheva, Panchev, and Pancheva.
Reply to Pancheva, Panchev, and Pancheva.
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回复潘切瓦、潘切夫和潘切瓦。
DOI:
10.1152/japplphysiol.00449.2013
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发表时间:
2013
影响因子:
3.3
通讯作者:
Jue T.
中科院分区:
文献类型:
--
作者:
Masuda K;Yamada T;Jue T.
TO THE EDITOR: we appreciate the feedback and the provocative comments of Dr. Pancheva and coworkers (2). On the basis of our recent study showing a direct interaction of Mb with mitochondria, Dr. Pancheva et al. proposed a theory about the immediate metabolism of oxygen, ATP, and PCr during muscle contraction: electrical current enhances O2 “detachment” from heme, mechanical contraction facilitates O2 release and allows Mb to serve as an excessive O2 scavenger, elevated temperature decreases O2 affinity of Mb, and CO2 induces Bohr effect in Mb.The literature does contain a long history of reports that would cast invaluable perspectives on Pancheva et al.’s theory (3). Many studies have examined how electrostatics help Mb discriminate ligand binding and how the electric field could affect Mb movement. These studies, however, do not claim that a physiologically relevant electric field can alter the heme Fe-O2 covalent bond and facilitate the O2 “detachment” from the heme. In fact, many studies focus on the electrostatic effect on the ligand migration, which the authors’ restrictive definition of diffusion would appear to preclude (5). Although a mechanical-chemical coupling could alter the Mb function, NMR studies suggest a minimal role for an overall protein effect, as implied in Pancheva et al.’s theory (1). The heme environment responds only to very high pressure to change the protein volume. How the discussion of mechanical-chemical coupling leads to evidence supporting the role of Mb as an O2 scavenger seems unclear. Studies have already shown that increasing the temperature from 30 C to 35 C will decrease slightly the O2 affinity of Mb,
影响因子:
3.3
作者:
Adelina V. Pancheva;Vladimir S. Panchev;M. Pancheva
通讯作者:
M. Pancheva
影响因子:
--
作者:
H. Kontos;D. Richardson;J. Patterson
通讯作者:
J. Patterson