Structural basis of inter-protein electron transfer for nitrite reduction in denitrification (Q27658068)

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Takuya Nakagami

3

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Kazuo Kobayashi

4

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Tsuyoshi Inoue

5

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Kazuya Yamaguchi

6

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Shinnichiro Suzuki

Emendation of genus Achromobacter and Achromobacter xylosoxidans (Yabuuchi and Yano) and proposal of Achromobacter ruhlandii (Packer and Vishniac) comb. nov., Achromobacter piechaudii (Kiredjian et al.) comb. nov., and Achromobacter xylosoxidans sub

7

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language of work or name

English

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publication date

5 November 2009

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published in

Nature

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volume

462

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issue

7269

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page(s)

117-20

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cites work

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Atomic Resolution Structures of Native Copper Nitrite Reductase from Alcaligenes xylosoxidans and the Active Site Mutant Asp92Glu

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Site-directed mutagenesis of azurin from Pseudomonas aeruginosa enhances the formation of an electron-transfer complex with a copper-containing nitrite reductase from Alcaligenes faecalis S-6

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Two c-type cytochromes, NirM and NirC, encoded in the nir gene cluster of Pseudomonas aeruginosa act as electron donors for nitrite reductase

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Characterization of nitrite reductase from a denitrifier, Alcaligenes sp. NCIB 11015. A novel copper protein.

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Copper-containing nitrite reductase from Pseudomonas aureofaciens is functional in a mutationally cytochrome cd1-free background (NirS-) of Pseudomonas stutzeri

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Metal coordination and mechanism of multicopper nitrite reductase

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Pseudospecific docking surfaces on electron transfer proteins as illustrated by pseudoazurin, cytochrome c550 and cytochrome cd1 nitrite reductase

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