Literature summary for 1.7.2.1 extracted from

Sasaki, D.; Watanabe, T.F.; Eady, R.R.; Garratt, R.C.; Antonyuk, S.V.; Hasnain, S.S.
Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes (2020), IUCrJ, 7, 557-565 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
the type 1 copper in the N-terminal tethered cupredoxin domain is placed too far away from the catalytic core type i copper for effective electron transfer. The N-terminal peptide that carries His27 plays a role in water-mediated anchoring of the substrate at the type 2 copper site	Hyphomicrobium denitrificans

Protein Variants

Protein Variants	Comment	Organism
additional information	the core type 1 copper mutant displays a long-range electron tunneling route via a hydrophobic beta-strand, thereby bypassing the type 1 copper core and delivering electrons directly to the catalytic type 2 copper center	Hyphomicrobium denitrificans

Metals/Ions

Metals/Ions	Comment	Organism	Structure
copper	-	Hyphomicrobium denitrificans

Organism

Organism	UniProt	Comment	Textmining
Hyphomicrobium denitrificans	N0B9M5	-	-
Hyphomicrobium denitrificans 1NES1	N0B9M5	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Hyphomicrobium denitrificans

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
nitrite + reduced phenazine methosulfate	-	Hyphomicrobium denitrificans	NO + oxidized phenazine methosulfate	-	?
nitrite + reduced phenazine methosulfate	-	Hyphomicrobium denitrificans 1NES1	NO + oxidized phenazine methosulfate	-	?

Subunits

Subunits	Comment	Organism
hexamer	crystallization data	Hyphomicrobium denitrificans

Synonyms

Synonyms	Comment	Organism
HYPDE_25578	-	Hyphomicrobium denitrificans

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Release 2023.1 (January 2023)