Literature summary for 1.7.2.5 extracted from

Pisliakov, A.; Hino, T.; Shiro, Y.; Sugita, Y.
Molecular dynamics simulations reveal proton transfer pathways in cytochrome C-dependent nitric oxide reductase (2012), PLoS Comput. Biol., 8, e1002674.

Crystallization (Commentary)

Crystallization (Comment)	Organism
all-atom molecular dynamics simulations within an explicit membrane/solvent environment reveal two possible proton transfer pathways leading from the periplasm to the active site, while no pathways from the cytoplasmic side are found, consistently with the experimental observations that the enzyme is not a proton pump. One of the pathways is blocked in the crystal structure and requires small structural rearrangements to allow for water channel formation. That pathway is equivalent to the functional periplasmic cavity postulated in cbb3 oxidase	Pseudomonas aeruginosa

Crystallization (Comment)

Organism

all-atom molecular dynamics simulations within an explicit membrane/solvent environment reveal two possible proton transfer pathways leading from the periplasm to the active site, while no pathways from the cytoplasmic side are found, consistently with the experimental observations that the enzyme is not a proton pump. One of the pathways is blocked in the crystal structure and requires small structural rearrangements to allow for water channel formation. That pathway is equivalent to the functional periplasmic cavity postulated in cbb3 oxidase

Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	Q59646	nitric oxide reductase subunit C	-
Pseudomonas aeruginosa ATCC 15692	Q59646	nitric oxide reductase subunit C	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	all-atom molecular dynamics simulations within an explicit membrane/solvent environment reveal two possible proton transfer pathways leading from the periplasm to the active site, while no pathways from the cytoplasmic side are found, consistently with the experimental observations that the enzyme is not a proton pump. One of the pathways is blocked in the crystal structure and requires small structural rearrangements to allow for water channel formation. That pathway is equivalent to the functional periplasmic cavity postulated in cbb3 oxidase	Pseudomonas aeruginosa	?	-	?
additional information	all-atom molecular dynamics simulations within an explicit membrane/solvent environment reveal two possible proton transfer pathways leading from the periplasm to the active site, while no pathways from the cytoplasmic side are found, consistently with the experimental observations that the enzyme is not a proton pump. One of the pathways is blocked in the crystal structure and requires small structural rearrangements to allow for water channel formation. That pathway is equivalent to the functional periplasmic cavity postulated in cbb3 oxidase	Pseudomonas aeruginosa ATCC 15692	?	-	?