Heme orientational disorder in reconstituted and native sperm whale myoglobin

Mar, Gerd N. La; Davis, Nicolette L.; Parish, Daniel W.; Smith, Kevin M.

doi:10.1016/s0022-2836(83)80080-1

Cited by 161 publications

(52 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…First, 1 H NMR study of reconstituted native myoglobin with protoheme-IX revealed that there are two interconverting protein forms in solution which differ in the orientation of the heme by a 180°rotation around the a,c-meso axis [4]. One of the orientational isomers has a higher stability than the other, and it dominates over times, after the reconstitution of myoglobin [5,6]. Furthermore, several years ago, the myoglobin reconstitution work in Neya's laboratory revealed after insertion in apomyoglobin that both iron porphine [7] and iron octamethylporphyrin [8] rotate freely about the iron-histidine bond whereas with iron octaethylporphyrin [9] and etiohemin [10], no rotation of the artificial prosthetic group was observed.…”

Section: Introductionmentioning

confidence: 99%

Proton NMR study of myoglobin reconstituted with 3,7-diethyl-2,8-dimethyl iron porphyrin: Remarkable influence of peripheral substitution on heme rotation

Juillard¹,

Bondon²,

Simonneaux³

2006

Journal of Inorganic Biochemistry

View full text Add to dashboard Cite

Section: Introductionmentioning

confidence: 99%

Proton NMR study of myoglobin reconstituted with 3,7-diethyl-2,8-dimethyl iron porphyrin: Remarkable influence of peripheral substitution on heme rotation

Juillard¹,

Bondon²,

Simonneaux³

2006

Journal of Inorganic Biochemistry

View full text Add to dashboard Cite

“…In all cases, two sets of resonances are detected per protein. These arise from the heme rotational isomers, which typically exchange slowly on the chemical shift time scale [48, 49]. Assignments of most heme resonances of both isomers in WT CtrHb and the T111H and L75H variants were obtained by established procedures [50].…”

Section: Resultsmentioning

confidence: 99%

Introduction of a covalent histidine–heme linkage in a hemoglobin: A promising tool for heme protein engineering

Rice

Preimesberger

Johnson

et al. 2014

Journal of Inorganic Biochemistry

View full text Add to dashboard Cite

The hemoglobins of the cyanobacteria Synechococcus and Synechocystis (GlbNs) are capable of spontaneous and irreversible attachment of the b heme to the protein matrix. The reaction, which saturates the heme 2-vinyl by addition of a histidine residue, is reproduced in vitro by preparing the recombinant apoprotein, adding ferric heme, and reducing the iron to the ferrous state. Spontaneous covalent attachment of the heme is potentially useful for protein engineering purposes. Thus, to explore whether the histidine–heme linkage can serve in such applications, we attempted to introduce it in a test protein. We selected as our target the heme domain of Chlamydomonas eugametos LI637 (CtrHb), a eukaryotic globin that exhibits less than 50% sequence identity with the cyanobacterial GlbNs. We chose two positions, 75 in the FG corner and 111 in the H helix, to situate a histidine near a vinyl group. We characterized the proteins with gel electrophoresis, absorbance spectroscopy, and NMR analysis. Both T111H and L75H CtrHbs reacted upon reduction of the ferric starting material containing cyanide as the distal ligand to the iron. With L75H CtrHb, nearly complete (> 90%) crosslinking was observed to the 4-vinyl as expected from the X-ray structure of wild-type CtrHb. Reaction of T111H CtrHb also occurred at the 4-vinyl in a 60% yield, indicating a preference for the flipped heme orientation in the starting material. The work suggests that the His–heme modification will be applicable to the design of proteins with a non-dissociable heme group.

show abstract

“…La Mar et al [8] have shown that in normal myoglobin about 8 % of the hemes are disordered in the sense that they are rotated 180°around the a-T-meso axis with respect to the position indicated by crystallographic data. A similar situation may be present in hemoglobin systems.…”

Section: Discussionmentioning

confidence: 99%

<title>Heme-tryptophan relationships in hemoglobin explored by frequency-domain time-resolved fluorescence at 10-GHz resolution</title>

et al. 1992

View full text Add to dashboard Cite

We measured the time-resolved fluorescence spectroscopy of human and bovine oxy-and deoxyhemoglobins in either 0.03 M phosphate buffer or 0.03 M borate buffer between pH 6.5 and 9.2. A frequency resolved fluorometer was used with bandwidth up to 10 GHz. Excitation was at 294 nm, the emission was monitored through a broad band interference filter centered at 335 nm, coupled to a cut-off filter at 316 nm. In all cases, the best simulations were obtained with two discrete exponential decays, one near 30 ps, and the other of several hundred ps. In human hemoglobin, the longer component showed a substantial lengthening upon removal of oxygen. In bovine hemoglobin, the shorter component decreased upon deoxygenation. It was possible to infer that the shorter lifetimes originated from the average intrachain distances of tryptophans and hemes. Instead, the longer lifetimes were consistent with the interchain distances. However, the hemes at this longer distance would become the main acceptors of energy transfer only when the energy transfer at intrasubunit distance is inhibited. It is suggested that this is due to the presence of "disordered" heme in the system.

show abstract

Heme orientational disorder in reconstituted and native sperm whale myoglobin

Cited by 161 publications

References 20 publications

Proton NMR study of myoglobin reconstituted with 3,7-diethyl-2,8-dimethyl iron porphyrin: Remarkable influence of peripheral substitution on heme rotation

Proton NMR study of myoglobin reconstituted with 3,7-diethyl-2,8-dimethyl iron porphyrin: Remarkable influence of peripheral substitution on heme rotation

Introduction of a covalent histidine–heme linkage in a hemoglobin: A promising tool for heme protein engineering

<title>Heme-tryptophan relationships in hemoglobin explored by frequency-domain time-resolved fluorescence at 10-GHz resolution</title>

Contact Info

Product

Resources

About