Heme-protein interactions in cytochrome c peroxidase revealed by site-directed mutagenesis and resonance Raman spectra of isotopically labeled hemes

Smulevich, Giulietta; Hu, Songzhou; Rodgers, Kenton R.; Goodin, David B.; Smith, Kevin M.; Spiro, Thomas G.

doi:10.1002/(sici)1520-6343(1996)2:6<365::aid-bspy3>3.0.co;2-2

Cited by 86 publications

(130 citation statements)

References 38 publications

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“…The band at 396 cm -1 in the spectrum of the ferric form of the protein falls between the frequency regions of the vinyl and the propionate bending modes and cannot be assigned without isotopic labelling of the heme. Although vinyl modes with a comparable low frequency have been observed for isotopically labelled cytochrome c peroxidase 30 and Mb, 26 the difference in frequency between the 396 cm -1 and the 436 cm -1 bands is, to our knowledge, higher than normally observed for the splitting of the vinyl modes of other hemeproteins. 31 In the RR spectrum of the ferrous form of GsGCS 162 a band appears at 404 cm -1 .…”

Section: Resonance Raman Spectroscopysupporting

confidence: 40%

HisE11 and HisF8 Provide Bis-histidyl Heme Hexa-coordination in the Globin Domain of Geobacter sulfurreducens Globin-coupled Sensor

Pesce¹,

Thijs

Nardini

et al. 2009

Journal of Molecular Biology

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⁎Among heme-based sensors, recent phylogenomic and sequence analyses have identified 34 globin coupled sensors (GCS), to which an aerotactic or gene-regulating function has been tentatively ascribed. Here, the structural and biochemical characterization of the globin domain of the GCS from Geobacter sulfurreducens (GsGCS 162 ) is reported. A combination of X-ray crystallography (crystal structure at 1.5 Å resolution), UV-vis and resonance Raman spectroscopy reveals the ferric GsGCS 162 as an example of bishistidyl hexa-coordinated GCS. In contrast to the known hexa-coordinated globins, the distal heme-coordination in ferric GsGCS 162 is provided by a His residue unexpectedly located at the E11 topological site. Furthermore, UV-vis and resonance Raman spectroscopy indicated that ferrous deoxygenated GsGCS 162 is a penta-/hexa-coordinated mixture, and the heme hexa-to-penta-coordination transition does not represent a rate-limiting step for carbonylation kinetics. Lastly, electron paramagnetic resonance indicates that ferrous nitrosylated GsGCS 162 is a penta-coordinated species, where the proximal HisF8-Fe bond is severed. Abbreviations used: GCS, globin-coupled sensor; GsGCS 162 , globin domain of GCS from Geobacter sulfurreducens; PAS, an acronym formed from the names of the first three proteins (the Period clock protein of Drosophila, the Aryl hydrocarbon receptor nuclear translocator of vertebrates, and the Single-minded protein of Drosophila) recognized as sharing such sensor motif; CooA, transcriptional activator of coo operons encoding proteins required to metabolize CO as a sole energy

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Section: Resonance Raman Spectroscopysupporting

confidence: 40%

HisE11 and HisF8 Provide Bis-histidyl Heme Hexa-coordination in the Globin Domain of Geobacter sulfurreducens Globin-coupled Sensor

Pesce¹,

Thijs

Nardini

et al. 2009

Journal of Molecular Biology

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“…Among them, 1562 cm À1 is attributed to C C stretching vibration, 1580 cm À1 is attributed to phenylalanine and C C m asymmetrical stretching mode 9 which also have contribution to 1621 cm À1 . These highfrequency peaks have been reliably related to vinyl group planarity with respect to the porphyrin core, by Smulevich et al 12 So, the high blood glucose level not only has in°uenced on protein function, but also a®ects the heme's structure. More detailed assignments of all peaks are shown in Table 1.…”

Section: Discussionmentioning

confidence: 90%

Raman Spectroscopy of Human Hemoglobin for Diabetes Detection

Lin

Huang

et al. 2014

J. Innov. Opt. Health Sci.

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Glycated hemoglobin (HbA1c) has been increasingly accepted as the gold standard for diabetes monitoring. In this study, Raman spectroscopy was tentatively employed for human hemoglobin (Hb) biochemical analysis aimed at developing a simple blood test for diabetes monitoring. Raman spectroscopy measurements were performed on hemoglobin samples of patients (n ¼ 39) with con¯rmed diabetes and healthy volunteers (n ¼ 37). The tentative assignments of the measured Raman bands were performed to compare the di®erence between these two groups. Meanwhile, principal component analysis (PCA) combined with linear discriminant analysis (LDA) were employed to develop e®ective diagnostic algorithms for classi¯cation between normal controls and patients with diabetes. As a result, the spectral features of these two groups demonstrated two distinct clusters with a sensitivity and speci¯city of 92.3% and 73%, respectively. Then the e®ec-tiveness of the diagnostic algorithm based on PCA-LDA technique was con¯rmed by receiver operating characteristic (ROC) curve. The area under the ROC curve was 0.92, indicating a good diagnostic result. In summary, our preliminary results demonstrate that proposing Raman spectroscopy can provide a signi¯cant potential for the noninvasive detection of diabetes.

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“…The most dramatic change was the appearance of a band at 327 cm Ϫ1 . This band is tentatively assigned to an out-of-plane mode ␥ 6 (pyrrole tilt) based on the frequency similarities with metMb (34), CCP (35), and TcAPII (36). Resonance enhancement of this mode was activated by doming of pentacoordinated hemes.…”

Section: Heme Iron Spin State and Coordinationmentioning

confidence: 87%

“…The heme is interacting with loop L1 on the other side via the coordination bond between iron and His 32 N⑀2 and through an H-bond network that involves the solvent-exposed propionates and residues His 32 , Asn 34 , and Gly 35 . The presence of the heme provides a link between L1 and L2.…”

Section: Discussionmentioning

confidence: 99%

“…However, substitution of the axial Tyr 75 ligand with a nonbonding alanine surely affected the electronic structure of the iron(III) center. Significant chemical shift changes were observed for the signals of Gly 35 , Asn 36 , Asn 79 , and Ala 82 , which were located in well resolved regions of the spectrum of holoHasA WT . Furthermore, in holo-Y75A, splitting was observed for most of the signals in the surrounding of the heme.…”

Section: Y75a Mutantmentioning

confidence: 93%

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