Haem and Non-Haem Iron in British Household Diets

1980 ◽  
Vol 34 (2) ◽  
pp. 141-145
Author(s):  
Nicola L Bull ◽  
D. H. Buss
Keyword(s):  
1999 ◽  
Vol 34 ◽  
pp. 51-69 ◽  
Author(s):  
Issa S. Isaac ◽  
John H. Dawson
Keyword(s):  

2021 ◽  
Vol 14 (1) ◽  
Author(s):  
Siddhartha Kundu

Abstract Objective Non-haem iron(II)- and 2-oxoglutarate-dependent dioxygenases (i2OGdd), are a taxonomically and functionally diverse group of enzymes. The active site comprises ferrous iron in a hexa-coordinated distorted octahedron with the apoenzyme, 2-oxoglutarate and a displaceable water molecule. Current information on novel i2OGdd members is sparse and relies on computationally-derived annotation schema. The dissimilar amino acid composition and variable active site geometry thereof, results in differing reaction chemistries amongst i2OGdd members. An additional need of researchers is a curated list of sequences with putative i2OGdd function which can be probed further for empirical data. Results This work reports the implementation of $$Fe\left(2\right)OG$$ F e 2 O G , a web server with dual functionality and an extension of previous work on i2OGdd enzymes $$\left(Fe\left(2\right)OG\equiv \{H2OGpred,DB2OG\}\right)$$ F e 2 O G ≡ { H 2 O G p r e d , D B 2 O G } . $$Fe\left(2\right)OG$$ F e 2 O G , in this form is completely revised, updated (URL, scripts, repository) and will strengthen the knowledge base of investigators on i2OGdd biochemistry and function. $$Fe\left(2\right)OG$$ F e 2 O G , utilizes the superior predictive propensity of HMM-profiles of laboratory validated i2OGdd members to predict probable active site geometries in user-defined protein sequences. $$Fe\left(2\right)OG$$ F e 2 O G , also provides researchers with a pre-compiled list of analyzed and searchable i2OGdd-like sequences, many of which may be clinically relevant. $$Fe(2)OG$$ F e ( 2 ) O G , is freely available (http://204.152.217.16/Fe2OG.html) and supersedes all previous versions, i.e., H2OGpred, DB2OG.


Nature ◽  
2021 ◽  
Author(s):  
Wupeng Yan ◽  
Heng Song ◽  
Fuhang Song ◽  
Yisong Guo ◽  
Cheng-Hsuan Wu ◽  
...  
Keyword(s):  

2017 ◽  
Vol 19 (44) ◽  
pp. 30107-30119 ◽  
Author(s):  
G. Rugg ◽  
H. M. Senn
Keyword(s):  

All O2 activation roads for three substrates and three spin states in SyrB2 lead to the same [FeO] structure.


1992 ◽  
Vol 144 (3) ◽  
pp. 235-257 ◽  
Author(s):  
C.M. Morris ◽  
J.M. Candy ◽  
A.E. Oakley ◽  
C.A. Bloxham ◽  
J.A. Edwardson
Keyword(s):  

1991 ◽  
Vol 43 (2-3) ◽  
pp. 129
Author(s):  
M.R. Cheesman ◽  
F.H.A. Kadir ◽  
G.R. Moore ◽  
A.J. Thomson ◽  
C. Greenwood ◽  
...  
Keyword(s):  

2012 ◽  
Vol 443 (2) ◽  
pp. 505-514 ◽  
Author(s):  
Davide Papale ◽  
Chiara Bruckmann ◽  
Ben Gazur ◽  
Caroline S. Miles ◽  
Christopher G. Mowat ◽  
...  

The vital signalling molecule NO is produced by mammalian NOS (nitric oxide synthase) enzymes in two steps. L-arginine is converted into NOHA (Nω-hydroxy-L-arginine), which is converted into NO and citrulline. Both steps are thought to proceed via similar mechanisms in which the cofactor BH4 (tetrahydrobiopterin) activates dioxygen at the haem site by electron transfer. The subsequent events are poorly understood due to the lack of stable intermediates. By analogy with cytochrome P450, a haem-iron oxo species may be formed, or direct reaction between a haem-peroxy intermediate and substrate may occur. The two steps may also occur via different mechanisms. In the present paper we analyse the two reaction steps using the G586S mutant of nNOS (neuronal NOS), which introduces an additional hydrogen bond in the active site and provides an additional proton source. In the mutant enzyme, BH4 activates dioxygen as in the wild-type enzyme, but an interesting intermediate haem species is then observed. This may be a stabilized form of the active oxygenating species. The mutant is able to perform step 2 (reaction with NOHA), but not step 1 (with L-arginine) indicating that the extra hydrogen bond enables it to discriminate between the two mono-oxygenation steps. This implies that the two steps follow different chemical mechanisms.


Tetrahedron ◽  
2012 ◽  
Vol 68 (15) ◽  
pp. 3231-3236 ◽  
Author(s):  
Victoria J. Dungan ◽  
Shwo Mun Wong ◽  
Sarah M. Barry ◽  
Peter J. Rutledge
Keyword(s):  

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