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Keywords: haem
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Biochem J (2015) 467 (1): 153–165.
Published: 20 March 2015
... B have been deposited in the PDB under code 4JS9. 29 10 2014 23 12 2014 22 1 2015 22 1 2015 © The Authors Journal compilation © 2015 Biochemical Society 2015 Nitric oxide synthases (NOSs) are haem-thiolate enzymes that catalyse the conversion of L -arginine ( L...
Includes: Supplementary data
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Biochem J (2013) 449 (1): 69–78.
Published: 07 December 2012
...Rafał R. Starzyński; François Canonne-Hergaux; Małgorzata Lenartowicz; Wojciech Krzeptowski; Alexandra Willemetz; Agnieszka Styś; Joanna Bierła; Piotr Pietrzak; Tomasz Dziaman; Paweł Lipiński HO1 (haem oxygenase 1) and Fpn (ferroportin) are key proteins for iron recycling from senescent red blood...
Includes: Supplementary data
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Biochem J (2012) 448 (2): 253–260.
Published: 07 November 2012
...Michael L. Ginger; Katharine A. Sam; James W. A. Allen Mitochondrial cytochromes c and c 1 are core components of the respiratory chain of all oxygen-respiring eukaryotes. These proteins contain haem, covalently bound to the polypeptide in a catalysed post-translational modification. In all...
Includes: Supplementary data
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Biochem J (2012) 445 (2): 175–182.
Published: 27 June 2012
...’. However, the three side chains of Lys 92 , Lys 118 and Lys 130 that were reported to be involved in covalent chromophore binding appear to be freely accessible to ligands accommodated in the hydrophobic pocket. A structural feature similar to the well-known Cys–Pro haem-binding motif indicates...
Includes: Supplementary data
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Biochem J (2012) 442 (2): 335–343.
Published: 13 February 2012
...Helge K. Abicht; Jacobo Martinez; Gunhild Layer; Dieter Jahn; Marc Solioz Lactococcus lactis cannot synthesize haem, but when supplied with haem, expresses a cytochrome bd oxidase. Apart from the cydAB structural genes for this oxidase, L. lactis features two additional genes, hemH and hemW ( hemN...
Includes: Supplementary data
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Biochem J (2012) 441 (1): 473–480.
Published: 14 December 2011
... were returned to normal and haem synthesis was restored. In mitochondria carrying the mutant Isu1 and no frataxin, Fe–S cluster enzyme activities were improved. The efficiency of new Fe–S cluster synthesis in isolated mitochondria was markedly increased compared with frataxin-negative cells, although...
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Biochem J (2011) 440 (1): 137–146.
Published: 27 October 2011
...Heeyong Yoon; Yan Zhang; Jayashree Pain; Elise R. Lyver; Emmanuel Lesuisse; Debkumar Pain; Andrew Dancis Mitochondria transport and utilize iron for the synthesis of haem and Fe–S clusters. Although many proteins are known to be involved in these processes, additional proteins are likely...
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Biochem J (2011) 434 (1): 105–111.
Published: 27 January 2011
... of supporting its growth in the presence of haem as the sole iron supply. In addition, when trophozoites were maintained in cultures supplemented with haemoglobin as the only iron source, the haem was released and thus it was introduced into cells. Interestingly, the Ehhmbp26 and Ehhmbp45 proteins could...
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Biochem J (2010) 425 (1): 257–264.
Published: 14 December 2009
... A), a homologue of Streptococcus pyogenes streptopain (SpeB). The role of InpA in haemoglobin breakdown and haem release was investigated. At pH 7.5, InpA mediated oxidation of oxyhaemoglobin to hydroxymethaemoglobin [in which the haem iron is oxidized to the Fe(III) state and which carries OH − as the sixth co...
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Biochem J (2009) 422 (2): 237–246.
Published: 13 August 2009
...Maria G. Mason; Peter Nicholls; Chris E. Cooper The steady-state behaviour of isolated mammalian cytochrome c oxidase was examined by increasing the rate of reduction of cytochrome c . Under these conditions the enzyme's 605 (haem a ), 655 (haem a 3 /Cu B ) and 830 (Cu A ) nm spectral features...
Includes: Supplementary data
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Biochem J (2009) 420 (1): 17–25.
Published: 28 April 2009
... Figure S1 at http://www.BiochemJ.org/bj/420/bj420017add.htm ). For example, there is 60% similarity and 43% identity between the deaminases from Escherichia coli and humans [ 6 ] (see Figure 1 ). PBGD from E. coli was the first haem biosynthesis enzyme structure to be solved, initially at 1.90 Å (1...
Includes: Supplementary data
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Biochem J (2009) 418 (3): 691–700.
Published: 25 February 2009
... is comparable with various animal NOSs, none of the exon–intron boundaries are conserved. Recombinant expression of clones with various N-termini identified N-terminal amino acids essential for enzyme activity, but not required for haem binding or dimerization, and suggests the usage of non-AUG start codons...
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Biochem J (2009) 418 (1): 201–207.
Published: 28 January 2009
... are frequently found in the same organism. The genome of the filamentous cyanobacterium Anabaena ( Nostoc ) sp. PCC 7120 codes for three different fur genes. FurA is an essential protein involved in iron homoeostasis that also modulates dinitrogen fixation. FurA interacts with haem, impairing its DNA-binding...
Includes: Supplementary data
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Biochem J (2008) 414 (2): 177–187.
Published: 12 August 2008
... an oxidoreductase enzyme. 1 To whom correspondence should be addressed (email [email protected] ). 13 5 2008 11 6 2008 12 6 2008 © The Authors Journal compilation © 2008 Biochemical Society 2008 galactose glucose haem meiosis oxygen The Zn(II) 2 Cys 6...
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Biochem J (2007) 407 (1): 89–99.
Published: 12 September 2007
...Stefania Nicolis; Enrico Monzani; Chiara Ciaccio; Paolo Ascenzi; Luc Moens; Luigi Casella NGB (human neuroglobin), a recently discovered haem protein of the globin family containing a six-co-ordinated haem, is expressed in nervous tissue, but the physiological function of NGB is currently unknown...
Includes: Supplementary data
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Biochem J (2007) 401 (1): 235–245.
Published: 11 December 2006
...François J. M. Chartier; Manon Couture We report here the resonance Raman spectra of the FeIII–NO and FeII–NO complexes of the bacterial NOSs (nitric oxide synthases) from Staphylococcus aureus and Bacillus subtilis . The haem–NO complexes of these bacterial NOSs displayed Fe–N–O frequencies...
Includes: Supplementary data
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Biochem J (2006) 397 (1): 47–52.
Published: 14 June 2006
...Mark Shepherd; Tamara A. Dailey; Harry A. Dailey Protoporphyrin (IX) ferrochelatase catalyses the insertion of ferrous iron into protoporphyrin IX to form haem. These ferrochelatases exist as monomers and dimers, both with and without [2Fe-2S] clusters. The motifs for [2Fe-2S] cluster co-ordination...
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Biochem J (2005) 392 (2): 399–406.
Published: 22 November 2005
...), caspase-9 and other cofactors. The issue of whether the redox state of the haem in cyt c affects the initiation of the apoptotic pathway is currently a subject of debate. In a cell-free reconstitution system, we found that only oxidized cyt c was capable of activating the caspase cascade. Oxidized cyt c...
Includes: Supplementary data
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Biochem J (2005) 392 (1): 173–180.
Published: 08 November 2005
...Sridevi Kolluri; Timothy J. Sadlon; Brian K. May; Herbert L. Bonkovsky Haem is essential for the health and function of nearly all cells. 5-Aminolaevulinic acid synthase-1 (ALAS-1) catalyses the first and rate-controlling step of haem biosynthesis. ALAS-1 is repressed by haem and is induced...
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Biochem J (2004) 378 (2): 599–607.
Published: 01 March 2004
... into rho°, consistent with secondary mitochondrial DNA damage from mitochondrial iron accumulation. In fact, in the Δ yhm1 mutant, iron was found to accumulate in mitochondria. The accumulated iron showed decreased availability for haem synthesis, measured in isolated mitochondria using endogenously...
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Biochem J (2000) 350 (2): 443–451.
Published: 23 August 2000
... . Oxygen-dependent modulation of mdr1b mRNA expression was prevented by actinomycin D, indicating transcriptional regulation. Inhibition of haem synthesis by 25 µ M CoCl 2 blocked mdr1b mRNA expression under both oxygen tensions, whereas 80 µ M desferrioxamine abolished modulation by O 2 . Haem (10 µ M...
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Biochem J (1999) 342 (2): 439–448.
Published: 24 August 1999
... terminal electron acceptor, but not in anaerobic cultures of the bacterium with other respiratory substrates. Ifc 3 was purified to homogeneity and revealed by biochemical, spectroscopic and primary structure analyses to contain four low-spin bis-His-ligated c 3 -haems, with midpoint reduction potentials...