Resonance Raman spectra of heme c and heme d1 in Pseudomonas cytochrome oxidase

Ching, Yuan-Chin; Ondrias, M. R.; Rousseau, Denis L.; Muhoberac, Barry B.; Wharton, David C.

doi:10.1016/0014-5793(82)80451-1

Cited by 22 publications

(11 citation statements)

References 25 publications

(31 reference statements)

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“…This pattern concurs with that of cytochrome cdl reductases [17,18]. (The -1340 cm-' band in the data of Ching et al [18] is obscured by a plasma line.)…”

Section: Predicted Vibrational Features Of Dionessupporting

confidence: 80%

“…This pattern concurs with that of cytochrome cdl reductases [17,18]. (The -1340 cm-' band in the data of Ching et al [18] is obscured by a plasma line.) Cotton et al [17] -1300-1410 cm-' region are also seen for siroheme iBCs [15,16] and bacteriochlorophylls [23].…”

Section: Predicted Vibrational Features Of Dionessupporting

confidence: 80%

“…This complex pattern thus appears characteristic of THPs as well as chlorins [12,14]. However, the most intense band in this region is at -1400 cm-' for iBCs [15,16,24] vs -1340 cm-' for the diones in this study and for the cdl reductases [17,18]. We are investigating the diagnostic utility of this difference.…”

Section: Predicted Vibrational Features Of Dionesmentioning

confidence: 68%

“…Much less is known about the vibrational properties of tetrahydroporphyrins (THP) such as iBCs or diones, although RR studies of sirohemes [15,16] and cytochrome cdl reductases [17,18] have been reported. For the latter, a 1715-1720-cm-' band in the RR was proposed as Y(C=O) of a keto group on the (then) presumed chlorin of heme dl [17,18].…”

Section: Resultsmentioning

confidence: 99%

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Modelling heme d₁

Andersson

Loehr

et al. 1990

FEBS Letters

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The heme d, macrocycle of Ps. aeruginosa dissimilatory nitrite reductase is an iron porphyrin-3,8-dione with a 17-acrylate substituent. We have compared the RR properties of Cu-d,, the copper(I1) TME of extracted heme d,, with those of models that differ only with respect to the acrylate: Cu-17-acrylate-mesoporphyrin-3,8-dione (2) and Cu-mesoporphyrin-3.8-dione (3). The RR spectrum of Cu-d, is very similar to that of 2, including v(C = 0) at _ 1720 cm-I. Replacement of the acrylate with propionate changes the spectrum markedly. For example, the v(C = 0) mode of 3 shifts to 1712 cn-i, and peaks of Cu-d, and 2 at u 1400 and N 1535 cn-i are shifted or absent from the spectrum of 3. FTIR spectra of 2 and 3 also differ in their v,,(C = 0) frequencies. The acrylate thus has a surprisingly strong influence on the electronic structural and spectral properties of heme d,. These data provide a foundation for studies of the novel biological porphyrindione macrocycles.

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“…This pattern concurs with that of cytochrome cdl reductases [17,18]. (The -1340 cm-' band in the data of Ching et al [18] is obscured by a plasma line.)…”

Section: Predicted Vibrational Features Of Dionessupporting

confidence: 80%

Section: Predicted Vibrational Features Of Dionessupporting

confidence: 80%

Section: Predicted Vibrational Features Of Dionesmentioning

confidence: 68%

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

Modelling heme d₁

Andersson

Loehr

et al. 1990

FEBS Letters

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“…Note that differences between the spectrum in Fig. 3A and a spectrum of oxidized cd 1 published previously (25) are likely to be due to different excitation lines and temperatures.…”

Section: Resultsmentioning

confidence: 69%

NirN Protein from Pseudomonas aeruginosa is a Novel Electron-bifurcating Dehydrogenase Catalyzing the Last Step of Heme d1 Biosynthesis

Adamczack

Hoffmann

Papke

et al. 2014

Journal of Biological Chemistry

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Heme d1 plays an important role in denitrification as the essential cofactor of the cytochrome cd1 nitrite reductase NirS. At present, the biosynthesis of heme d1 is only partially understood. The last step of heme d1 biosynthesis requires a so far unknown enzyme that catalyzes the introduction of a double bond into one of the propionate side chains of the tetrapyrrole yielding the corresponding acrylate side chain. In this study, we show that a Pseudomonas aeruginosa PAO1 strain lacking the NirN protein does not produce heme d1. Instead, the NirS purified from this strain contains the heme d1 precursor dihydro-heme d1 lacking the acrylic double bond, as indicated by UV-visible absorption spectroscopy and resonance Raman spectroscopy. Furthermore, the dihydro-heme d1 was extracted from purified NirS and characterized by UV-visible absorption spectroscopy and finally identified by high-resolution electrospray ionization mass spectrometry. Moreover, we show that purified NirN from P. aeruginosa binds the dihydro-heme d1 and catalyzes the introduction of the acrylic double bond in vitro. Strikingly, NirN uses an electron bifurcation mechanism for the two-electron oxidation reaction, during which one electron ends up on its heme c cofactor and the second electron reduces the substrate/product from the ferric to the ferrous state. On the basis of our results, we propose novel roles for the proteins NirN and NirF during the biosynthesis of heme d1.

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