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Efficient Electron Transfer in a Protein Network Lacking Specific Interactions
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DOI：10.1021/ja205043f.png)
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摘要
En 中文
In many biochemical processes, proteins need to bind partners amidst a sea of other molecules. Generally, partner selection is achieved by formation of a single-orientation complex with well-defined, short-range interactions. We describe a protein network that functions effectively in a metabolic electron transfer process but lacks such specific interactions. The soil bacterium Paracoccus denitrificans oxidizes a variety of compounds by channeling electrons into the main respiratory pathway. Upon conversion of methylamine by methylamine dehydrogenase, electrons are transported to the terminal oxidase to reduce molecular oxygen. Steady-state kinetic measurements and NMR experiments demonstrate a remarkable number of possibilities for the electron transfer, involving the cupredoxin amicyanin as well as four c-type cytochromes. The observed interactions appear to be governed exclusively by the electrostatic nature of each of the proteins. It is concluded that Paracoccus provides a pool of cytochromes for efficient electron transfer via weak, ill-defined interactions, in contrast with the view that functional biochemical interactions require well-defined molecular interactions. It is proposed that the lack of requirement for specificity in these interactions might facilitate the integration of new metabolic pathways.
Keyword:
CYTOCHROME-C-OXIDASE
MAU GENE-CLUSTER
PARACOCCUS-DENITRIFICANS
METHYLAMINE DEHYDROGENASE
CRYSTAL-STRUCTURE
TRANSFER COMPLEX
ENCOUNTER COMPLEX
NMR-SPECTROSCOPY
REDOX PROTEINS
AMICYANIN
期刊
IF:
15.6
论文数:
20.0W
被引数:
60.2W
机构
引用论文
Horizontal Transfer, Not Duplication, Drives the Expansion of Protein Families in Prokaryotes.png)
PLOS GENETICS
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PLOS GENETICSIF3.7
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