Porphyrins derived from the prosthetic group of myeloperoxidase

Nichol, A. W.; Morell, D.B.; Thomson, Judith

doi:10.1016/0006-291x(69)90343-x

Cited by 15 publications

(5 citation statements)

References 9 publications

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“…The simplest explanation of these three findings is that a single formyl group resides on ring III or IV, implying that 2,4-divinyl-8-(5)-formyl-deuteroporphyrin IX is the heme of myeloperoxidase. This conclusion is at variance with that of Nichol et al, who concluded that the carbonyl substituent of the myeloperoxidase heine is present on a two-carbon side chain [2].…”

Section: Discussioncontrasting

confidence: 60%

“…The identity of this linkage as amide bond would explain the resistance to clea~,age at the expense of methanolic HC1 [2] and HI in acetic acid [3]. An amide bond for heme has not previously been described, although other prosthetic groups are known to be attached in this manner.…”

Section: Discussionmentioning

confidence: 99%

“…While the nature of the linkages in cytochrome c and lactoperoxidase have been characterized, that present in myeloperoxidase remains unknown. Previous studies have, however, indicated that the linkage is not the heine c type [1] and that low yields of the prosthetic group are obtained with reagents which readily cleave ester bonds such as methanolic HC1 [2] and HI in acetic acid [3]. In this report we consider the possibility of an amide bond.…”

Section: Introductionmentioning

confidence: 89%

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The prosthetic group of myeloperoxidase

Wu¹,

Schultz²

1975

FEBS Letters

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Section: Discussioncontrasting

confidence: 60%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 89%

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The prosthetic group of myeloperoxidase

Wu¹,

Schultz²

1975

FEBS Letters

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“…Attempts to identify the iron-containing chromophores have been frustrated by their chemical instability (Harrison & Schultz, 1978; Wu & Schultz, 1975;Nichol et al, 1969; Odajima & Yamazaki, 1972b;Newton et al, 1965a,b). The prosthetic groups are covalently linked to the protein (Wu & Schultz, 1975;Schultz et al, 1983).…”

mentioning

confidence: 99%

“…The prosthetic groups are covalently linked to the protein (Wu & Schultz, 1975;Schultz et al, 1983). Under conditions examined thus far, cleavage has led to isolation of hemes with physical properties that are distinctly altered from the native enzyme (Harrison & Schultz, 1978;Wu & Schultz, 1975;Nichol et al, 1969). Structural identification has therefore relied principally upon inference from physical characteristics of the intact enzyme.…”

mentioning

confidence: 99%

Structural analysis of myeloperoxidase by resonance Raman spectroscopy

Sibbett¹,

Hurst²

1984

Biochemistry

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Soret excitation of canine myeloperoxidase (MPO) gives rise to a complex resonance Raman (RR) spectrum characterized by multiple bands in the core size and oxidation state marker regions. Relative intensities of the bands obtained by 406- and 454-nm laser excitation were nearly identical and were temperature independent from 77 to 273 K. Spectra of dithionite-reduced and cyanide-coordinated derivatives are also reported. In the native and dithionite-reduced enzyme, there are no detectable bands between 1620 and 1700 cm-1, indicating that the hemes do not contain formyl substituents in conjugation with the macrocyclic ring. Excitation of the visible absorption band at 568 nm gave rise to only very weakly resonance-enhanced spectra. The RR spectra are interpreted within the context of other physical measurements to indicate that MPO contains two equivalent or nearly equivalent chlorin prosthetic groups. Possible mechanistic consequences of these structural features are discussed.

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Polycondensation of nucleotide analogues in the presence of imidazole

1973

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Oligomers of 3-(9-adenyl)-2-hydroxypropyl phosphate (I), 3-(3-adenyl)-2-hydroxypropyl phosphate (11) and 3-(7-theophillyl)-2-hydroxypropyl phosphate (111) were obtained by refluxing in DMF in the presence of imidazole or triethylamine hydrochloride. N-(2,3-Dihydroxypropyl) derivatives of the corresponding uucleic acid bases were formed as byproducts. The oligorners had higher molecular weights than those obtained by polycondensation using N,N-dicyclohexylcarbodiimide as dehydrating agent. ZUSAMMENFASSUNG:Oligomere von 3-(9-Adenyl)-2-hydroxypropylphosphat (I), 3-(3-Adenyl)-2-hydroxypropylphosphat (11) und 3-(7-Theophillyl)-2-hydroxypropylphosphat (111) wurden durch Kondensation in siedendern DMF in Gegenwart von Tmidazol oder Triathylhydrochlorid dargestellt. Als Nebenprodukt entstanden N-(2,3-Dihydroxypropyl)-Derivate der entsprechenden Nukleinsaure-Basen. Die Oligomeren hatten hohere Molekulargewichte als jene, die durch Polykondensation rnit N,N-Dicyclohexylcarbodiimid als Kondensationsmittel erhalten wurden.

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Porphyrins derived from the prosthetic group of myeloperoxidase

Cited by 15 publications

References 9 publications

The prosthetic group of myeloperoxidase

The prosthetic group of myeloperoxidase

Structural analysis of myeloperoxidase by resonance Raman spectroscopy

Polycondensation of nucleotide analogues in the presence of imidazole

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