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Keywords: non-haem iron
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Unexpected weak magnetic exchange coupling between haem and non-haem iron in the catalytic site of nitric oxide reductase (NorBC) from Paracoccus denitrificans

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Jessica H. Van Wonderen, Vasily S. Oganesyan, Nicholas J. Watmough, David J. Richardson, Andrew J. Thomson, Myles R. Cheesman
Journal: Biochemical Journal
Biochem J (2013) 451 (3): 389–394.
https://doi.org/10.1042/BJ20121406
Published: 12 April 2013
... transmembrane complex. The active site, in NorB, comprises high-spin haem b 3 in close proximity with non-haem iron, Fe B . In oxidized NorBC, the active site is EPR-silent owing to exchange coupling between Fe III haem b 3 and Fe B III (both S =5/2). On the basis of resonance Raman studies [Moënne-Loccoz...
View articletitled, Unexpected weak magnetic exchange coupling between haem and non-haem iron in the catalytic site of nitric oxide reductase (NorBC) from Paracoccus denitrificans
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Includes: Supplementary data
Articles

Biochemical characterization and mutational analysis of the mononuclear non-haem Fe 2+ site in Dke1, a cupin-type dioxygenase from Acinetobacter johnsonii

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Stefan Leitgeb, Grit D. Straganz, Bernd Nidetzky
Journal: Biochemical Journal
Biochem J (2009) 418 (2): 403–411.
https://doi.org/10.1042/BJ20081161
Published: 11 February 2009
... dioxygenase Dke1 metal site non-haem iron Non-haem Fe 2+ provides catalytic assistance to a variety of enzymatic reactions that utilize dioxygen as the co-substrate [ 1 – 5 ]. Contrasting with their functional diversity in these O 2 -dependent transformations, the protein metallocentres that bind...
View articletitled, Biochemical characterization and mutational analysis of the mononuclear non-haem Fe 2+ site in Dke1, a cupin-type dioxygenase from Acinetobacter johnsonii
Open the PDF for Biochemical characterization and mutational analysis of the mononuclear non-haem Fe 2+ site in Dke1, a cupin-type dioxygenase from Acinetobacter johnsonii in another window
Includes: Supplementary data
Articles

Substrate-induced conformational transition in human phenylalanine hydroxylase as studied by surface plasmon resonance analyses: the effect of terminal deletions, substrate analogues and phosphorylation

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Anne J. STOKKA, Torgeir FLATMARK
Journal: Biochemical Journal
Biochem J (2003) 369 (3): 509–518.
https://doi.org/10.1042/bj20021009
Published: 01 February 2003
[email protected] ). 28 6 2002 9 10 2002 15 10 2002 15 10 2002 The Biochemical Society, London ©2003 2003 conformational transition hysteresis non-haem iron phenylalanine hydroxylase surface plasmon resonance (SPR) Abbreviations used: BH 4 , (6 R )- l - erythro...
View articletitled, Substrate-induced conformational transition in human phenylalanine hydroxylase as studied by surface plasmon resonance analyses: the effect of terminal deletions, substrate analogues and phosphorylation
Open the PDF for Substrate-induced conformational transition in human phenylalanine hydroxylase as studied by surface plasmon resonance analyses: the effect of terminal deletions, substrate analogues and phosphorylation in another window