Proton NMR probes of the binuclear iron cluster in hemerythrin

1986 ◽  
Vol 108 (22) ◽  
pp. 6871-6879 ◽  
Author(s):  
Michael J. Maroney ◽  
Donald M. Kurtz ◽  
Judith M. Nocek ◽  
Linda L. Pearce ◽  
Lawrence. Que
Keyword(s):  
Proton Nmr ◽  
Iron Cluster ◽  
Binuclear Iron

NMR studies of porcine uteroferrin: Evidence for a spin-coupled binuclear iron cluster

1983 ◽  
Vol 79 ◽  
pp. 137
Author(s):  
L. Que ◽  
R.B. Lauffer ◽  
B.C. Antanaitis ◽  
P. Aisen
Keyword(s):  
Nmr Studies ◽  
Iron Cluster ◽  
Binuclear Iron

scholarly journals Rubrivivax gelatinosus acsF (Previously orf358) Codes for a Conserved, Putative Binuclear-Iron-Cluster-Containing Protein Involved in Aerobic Oxidative Cyclization of Mg-Protoporphyrin IX Monomethylester

2002 ◽  
Vol 184 (3) ◽  
pp. 746-753 ◽  
Author(s):  
Violaine Pinta ◽  
Martine Picaud ◽  
Françoise Reiss-Husson ◽  
Chantal Astier
Keyword(s):  
Fluorescence Emission ◽  
Growth Conditions ◽  
Oxidative Cyclization ◽  
Pharbitis Nil ◽  
Wild Type ◽  
Iron Cluster ◽  
Wide Range ◽  
Rubrivivax Gelatinosus ◽  
Respiratory Growth ◽  
Binuclear Iron

ABSTRACT This study describes the characterization of orf358, an open reading frame of previously unidentified function, in the purple bacterium Rubrivivax gelatinosus. A strain in which orf358 was disrupted exhibited a phenotype similar to the wild type under photosynthesis or low-aeration respiratory growth conditions. In contrast, under highly aerated respiratory growth conditions, the wild type still produced bacteriochlorophyll a (Bchl a), while the disrupted strain accumulated a compound that had the same absorption and fluorescence emission spectra as Mg-protoporphyrin but was less polar, suggesting that it was Mg-protoporphyrin monomethylester (MgPMe). These data indicated a blockage in Bchl a synthesis at the oxidative cyclization stage and implied the coexistence of two different mechanisms for MgPMe cyclization in R. gelatinosus, an anaerobic mechanism active under photosynthesis or low oxygenation and an aerobic mechanism active under high-oxygenation growth conditions. Based on these results as well as on sequence analysis indicating the presence of conserved putative binuclear-iron-cluster binding motifs, the designation of orf358 as acsF (for aerobic cyclization system Fe-containing subunit) is proposed. Several homologs of AcsF were found in a wide range of photosynthetic organisms, including Chlamydonomas reinhardtii Crd1 and Pharbitis nil PNZIP, suggesting that this aerobic oxidative cyclization mechanism is conserved from bacteria to plants.

ChemInform Abstract: 1H NMR Probes of the Binuclear Iron Cluster in Hemerythrin.

ChemInform ◽  
1987 ◽  
Vol 18 (12) ◽  
Author(s):  
M. J. MARONEY ◽  
D. M. JUN. KURTZ ◽  
J. M. NOCEK ◽  
L. L. PEARCE ◽  
L. JUN. QUE
Keyword(s):  
1H Nmr ◽  
Iron Cluster ◽  
Binuclear Iron

Isolation and characterization of rubrerythrin, a non-heme iron protein from Desulfovibrio vulgaris that contains rubredoxin centers and a hemerythrin-like binuclear iron cluster

Biochemistry ◽  
1988 ◽  
Vol 27 (5) ◽  
pp. 1636-1642 ◽  
Author(s):  
Jean LeGall ◽  
Benet C. Prickril ◽  
Isabel Moura ◽  
Antonio V. Xavier ◽  
Jose J. G. Moura ◽  
...  
Keyword(s):  
Heme Iron ◽  
Desulfovibrio Vulgaris ◽  
Iron Cluster ◽  
Iron Protein ◽  
Isolation And Characterization ◽  
Non Heme Iron ◽  
Binuclear Iron

Vasoactive intestinal contractor (VIC) peptide structure in solution as determinated by proton NMR

1992 ◽  
Vol 89 ◽  
pp. 175-181 ◽  
Author(s):  
A Aumelas ◽  
L Chiche ◽  
E Brun ◽  
E Mahé ◽  
D Le Nguyen ◽  
...  
Keyword(s):  
Proton Nmr ◽  
Peptide Structure ◽  
Structure In Solution

Benzene confined in MCM-41 below its melting point : A proton NMR study

2000 ◽  
Vol 10 (PR7) ◽  
pp. Pr7-99-Pr7-102 ◽  
Author(s):  
G. Dosseh ◽  
D. Morineau ◽  
C. Alba-Simionesco
Keyword(s):  
Melting Point ◽  
Proton Nmr ◽  
Nmr Study ◽  
Mcm 41
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