Coordination structure of the ferric heme iron in engineered distal histidine myoglobin mutants

Ikeda‐Saito, Masao; Hori, Hiroshi; Andersson, Laura A.; Prince, Roger C.; Pickering, Ingrid J.; George, Graham N.; Sanders, Charles R.; Lutz, Rodney S.; McKelvey, E.J.; Mattera, Rafael

doi:10.1016/s0021-9258(18)50024-7

Cited by 140 publications

(103 citation statements)

References 44 publications

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“…The 1 eV blue-shift of the absorption rising edge (feature A) and the decrease of the P pre-edge peak are both in agreement with the hypothesis that lipid-bound HMP is a high-spin Fe(III)-heme compound with a weakly interacting axial ligand. In particular, as discussed in a previous work (Boffi et al, 1999), the decrease of the P peak, is in agreement with the experimentally observed changes from a pentacoordinate to a hexacoordinate Fe-heme system (Oyanagy et al, 1987;Shiro et al, 1990;Ikeda-Saito et al, 1992). This peak probes empty molecular orbitals with d-symmetry and becomes evident when the asymmetry of the metal coordination increases due to p-d mixing.…”

Section: Xanes Spectrasupporting

confidence: 91%

Unusual Heme Iron-Lipid Acyl Chain Coordination in Escherichia coli Flavohemoglobin

D’Angelo

Lucarelli

Longa

et al. 2004

Biophysical Journal

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Escherichia coli flavohemoglobin is endowed with the notable property of binding specifically unsaturated and/or cyclopropanated fatty acids both as free acids or incorporated into a phospholipid molecule. Unsaturated or cyclopropanated fatty acid binding to the ferric heme results in a spectral change observed in the visible absorption, resonance Raman, extended x-ray absorption fine spectroscopy (EXAFS), and x-ray absorption near edge spectroscopy (XANES) spectra. Resonance Raman spectra, measured on the flavohemoglobin heme domain, demonstrate that the lipid (linoleic acid or total lipid extracts)-induced spectral signals correspond to a transition from a five-coordinated (typical of the ligand-free protein) to a hexacoordinated, high spin heme iron. EXAFS and XANES measurements have been carried out both on the lipid-free and on the lipid-bound protein to assign the nature of ligand in the sixth coordination position of the ferric heme iron. EXAFS data analysis is consistent with the presence of a couple of atoms in the sixth coordination position at 2.7 A in the lipid-bound derivative (bonding interaction), whereas a contribution at 3.54 A (nonbonding interaction) can be singled out in the lipid-free protein. This last contribution is assigned to the CD1 carbon atoms of the distal LeuE11, in full agreement with crystallographic data on the lipid-free protein at 1.6 A resolution obtained in the present work. Thus, the contributions at 2.7 A distance from the heme iron are assigned to a couple of carbon atoms of the lipid acyl chain, possibly corresponding to the unsaturated carbons of the linoleic acid.

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Section: Xanes Spectrasupporting

confidence: 91%

Unusual Heme Iron-Lipid Acyl Chain Coordination in Escherichia coli Flavohemoglobin

D’Angelo

Lucarelli

Longa

et al. 2004

Biophysical Journal

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“…To test the protein glycation of the HMb, we performed reactions with the D-ribose or D-glucose at 37 • C, pH 7.0, for 1-24 h. The UV-Vis spectra of the reaction solution were recorded at 1, 4, 8, 12, and 24 h, respectively. As shown in Figure S1A, the HMb exhibited the UV-Vis spectrum with characteristic absorption (Soret band, 409 nm; visible bands, ~500 and 630 nm), similar to that reported previously in pH 6.0 (409.5, 504, and 633 nm) [32]. Upon reaction with D-ribose or D-glucose, although the sugar did not cause blue-or red-shifts in the Soret band within 24 h, the D-ribose caused a large decrease in the intensity compared to that of the D-glucose (Figure S1B).…”

Section: Uv-vis Studiessupporting

confidence: 86%

“…The UV-Vis spectra of the HMb were recorded in 20 mmol/L potassium phosphate buffer (pH 7.0) on Agilent 8453 diode array spectrometer (Agilent Technologies, Inc., Santa Clara, CA, USA). The protein concentration was determined with an extinction coefficient of ε 409 = 153 L/mmol·cm [ 32 ]. The UV-Vis spectra of the HMb incubation with d -ribose or d -glucose were recorded before and after reacting for 1, 4, 8, 12, and 24 h, respectively.…”

Section: Methodsmentioning

confidence: 99%

Identification of the Protein Glycation Sites in Human Myoglobin as Rapidly Induced by d-Ribose

et al. 2021

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Protein glycation is an important protein post-translational modification and is one of the main pathogenesis of diabetic angiopathy. Other than glycated hemoglobin, the protein glycation of other globins such as myoglobin (Mb) is less studied. The protein glycation of human Mb with ribose has not been reported, and the glycation sites in the Mb remain unknown. This article reports that d-ribose undergoes rapid protein glycation of human myoglobin (HMb) at lysine residues (K34, K87, K56, and K147) on the protein surface, as identified by ultra-high performance liquid chromatography-mass spectrometry (UHPLC-MS) and electrospray ionization tandem mass spectrometry (ESI-MS/MS). Moreover, glycation by d-ribose at these sites slightly decreased the rate of the met heme (FeIII) in reaction with H2O2 to form a ferryl heme (FeIV=O). This study provides valuable insight into the protein glycation by d-ribose and provides a foundation for studying the structure and function of glycated heme proteins.

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“…For peroxidases, the reduction potential for the Fe(IV)/(III) redox equilibrium probably reflects catalytic activity [34]. However, the inherent instability of the Mb compound I ( [21] and references therein) has precluded the measurement of the midpoint potential for the Fe(IV)/(III) redox process in Mb.…”

Section: Discussionmentioning

confidence: 99%

“…Spectra of the wild-type Mb and the Y103F variant Mb prepared in phosphate buffer (100 mM, pH 7.4) showed Soret (λ max , 409 nm) and visible bands (λ max , 505-508 and 630-633 nm) similar to those of native Mb [33]. Where required, Mb solutions were quantified using the reported molar absorption coefficient ε 409 ∼153 × 10 3 M −1 • cm −1 [34].…”

Section: Electronic Absorption Spectramentioning

confidence: 99%

Regio- and stereo-chemical oxidation of linoleic acid by human myoglobin and hydrogen peroxide: Tyr103 affects rate and product distribution

Rayner

Stocker

Lay

et al. 2004

Biochemical Journal

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Mb (myoglobin) plus H2O2 catalyses the oxidation of various substrates via a peroxidase-like activity. A Y103F (Tyr103-->Phe) variant of human Mb has been constructed to assess the effect of exchanging an electron-rich oxidizable amino acid on the peroxidase activity of human Mb. Steady-state analyses of reaction mixtures containing Y103F Mb, purified linoleic acid and H2O2 revealed a lower total yield of lipid oxidation products than mixtures containing the wild-type protein, consistent with the reported decrease in the rate constant for reaction of Y103F Mb with H2O2 [Witting, Mauk and Lay (2002) Biochemistry 41, 11495-11503]. Irrespective of the Mb employed, lipid oxidation yielded 9(R/S)-HODE [9(R,S)-hydroxy-10E,12Z-octadecadienoic acid] in preference to 13(R/S)-HODE [13(R,S)-hydroxy-9Z,11E-octadecadienoic acid], while 9- and 13-keto-octadecadienoic acid were formed in trace amounts. However, lipid oxidation by the Y103F variant of Mb proceeded with a lower V(max) value and an increased K(m) value relative to the wild-type control. Consistent with the increased K(m), the product distribution from reactions with Y103F Mb showed decreased selectivity compared with the wild-type protein, as judged by the decreased yield of 9(S)-relative to 9(R)-HODE. Together, these data verify that Tyr103 plays a significant role in substrate binding and orientation in the haem pocket of human Mb. Also, the midpoint potential for the Fe(III)/(II) one-electron reduction was shifted slightly, but significantly, to a higher potential, confirming the importance of Tyr103 to the hydrogen-bonding network involving residues that line the haem crevice of human Mb.

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Coordination structure of the ferric heme iron in engineered distal histidine myoglobin mutants

Cited by 140 publications

References 44 publications

Unusual Heme Iron-Lipid Acyl Chain Coordination in Escherichia coli Flavohemoglobin

Unusual Heme Iron-Lipid Acyl Chain Coordination in Escherichia coli Flavohemoglobin

Identification of the Protein Glycation Sites in Human Myoglobin as Rapidly Induced by d-Ribose

Regio- and stereo-chemical oxidation of linoleic acid by human myoglobin and hydrogen peroxide: Tyr103 affects rate and product distribution

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