期刊
CHEMPHYSCHEM
卷 11, 期 6, 页码 1172-1180出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cphc.200900894
关键词
cyanobacteriochromes; photochemistry; photoreceptors; phytochromes; proteins
资金
- National Institutes of Health [GM068552]
- National Science Foundation Center for Biophotonics Science and Technology [PHY-0120999]
- National Science Foundation [MCB-08423625]
- Chemical Sciences, Geosciences, and Biosciences Division, Office of Basic Energy Sciences, Office of Science, United States Department of Energy (DOE ) [DE-FG02-09ER16117]
Photosensory proteins enable living things to detect the quantity and quality of the light environment and to transduce that physical signal into biochemical outputs which entrain their metabolism with the ambient light environment. Phytochromes, which photoconvert between red-absorbing P, and far-red-absorbing P-fr states, are the most extensively studied of these interesting proteins. Critical regulators of a number of key adaptive processes in higher plants, including photomorphogenesis and shade avoidance, phytochromes are widespread in photosynthetic and nonphotosynthetic bacteria, and even in fungi. Cyanobacterial genomes also possess a plethora of more distant relatives of phytochronnes known as cyanobacteriochromes (CBCRs). Biochemical characterization of representative CBCRs has demonstrated that this class of photosensors exhibits a broad range of wavelength sensitivities, spanning the entire visible spectrum. Distinct protein-bilin interactions are responsible for this astonishing array of wavelength sensitivities. Despite this spectral diversity, all members of the extended family of phytochrome photosensors appear to share a common photochemical mechanism for light sensing: photoisomerization of the 15/16 double bond of the bilin chromophore.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据