Compound I and II Analogs of a Chlorin

Jayaraj, K.; Gold, A.; Austin, Rachel N.; Mandon, Dominique; Weiß, Richard; Terner, James; Bill, Eckhard; Müther, Markus; Trautwein, Alfred X.

doi:10.1021/ja00140a030

Cited by 28 publications

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“…The considerable decrease in Soret extinction coefficient and almost total loss of spectral characteristics in the visible region when compared to the ferric enzyme are analogous to the spectral changes seen upon formation of HRP-I. Similar observations have been reported by Morishima (23), Gold (25) and their co-workers for compound I model compounds of iron tetramesitylchlorin and trans-2,3-dihydroxy-2,3-dimethyltetramesitylchlorin, respectively. Further comparison of the absorption spectra of MeChl-HRP-I and FIG.…”

Section: Compound I Of Iron Mechl-hrpsupporting

confidence: 84%

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Preparation and Initial Characterization of the Compound I, II, and III States of Iron Methylchlorin-Reconstituted Horseradish Peroxidase and Myoglobin: Models for Key Intermediates in Iron Chlorin Enzymes

Coulter

Cheek

Ledbetter

et al. 2000

Biochemical and Biophysical Research Communications

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Section: Compound I Of Iron Mechl-hrpsupporting

confidence: 84%

“…1). Aside from the oxoferryl heme d intermediate (12), previous studies of oxoferryl chlorins have examined tetraphenylchlorins model complexes in organic solvents at low temperatures (23)(24)(25). Stable oxyferrous iron chlorins derivatives have not been previously characterized (24).…”

mentioning

confidence: 99%

Preparation and Initial Characterization of the Compound I, II, and III States of Iron Methylchlorin-Reconstituted Horseradish Peroxidase and Myoglobin: Models for Key Intermediates in Iron Chlorin Enzymes

Coulter

Cheek

Ledbetter

et al. 2000

Biochemical and Biophysical Research Communications

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“…Another type of iron(IV) porphyrin isolated at that time was a dimethoxy derivative [65]. These compounds have been extensively studied and well characterized by various spectroscopic techniques, including visible spectroscopy, NMR, EPR (electron paramagnetic resonance), Mö ssbauer and EXAFS [65][66][67][68][69][70][71][72][73].…”

Section: Models and Mechanisms Of Oxidative Catalysis By Hemeiron Andmentioning

confidence: 99%

High-valent iron in chemical and biological oxidations

Groves

2006

Journal of Inorganic Biochemistry

577

477

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“…Whereas δ and ∆E Q values (Table 1) obtained from zero-field Mössbauer studies of the active oxidants in both haem and non-haem oxygenases are consistent with an iron(IV) oxidation state, the analysis of the Mössbauer spectra in an applied magnetic field reveals different spin states in the two cases. For haem enzymes the A tensor shows a qualitative trend of 'two large negative values, one small negative value' 20,21 , thereby reflecting an intermediate spin, S = 1 spin state for the iron(IV) centre. In CPd-I intermediates, this S = 1 spin state is coupled ferromagnetically or antiferromagnetically to the porphyrin radical cation, giving an overall quartet or doublet state, respectively 3,6,7,9 .…”

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confidence: 99%

The biology and chemistry of high-valent iron–oxo and iron–nitrido complexes

2012

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selective functionalization of unactivated c-H bonds and ammonia production are extremely important industrial processes. a range of metalloenyzmes achieve these challenging tasks in biology by activating dioxygen and dinitrogen using cheap and abundant transition metals, such as iron, copper and manganese. High-valent iron-oxo and -nitrido complexes act as active intermediates in many of these processes. the generation of well-described model compounds can provide vital insights into the mechanism of such enzymatic reactions. advances in the chemistry of model high-valent iron-oxo and -nitrido systems can be related to our understanding of the biological systems.H igh-valent oxoiron(IV) and formally oxoiron(V) species have been spectroscopically identified as active intermediates in the catalytic cycles of a number of enzymatic systems 1-10 . Haem and non-haem proteins use these reactive intermediates to couple the activation of dioxygen to the oxidation of their substrates. In most cases, an oxygen atom is inserted into an unactivated C-H bond of the substrate; for example, in hydroxylation reactions [1][2][3][4][5][6][7][8][9][10] . However, many other reactions, including halogenation, desaturation, cyclization, epoxidation and decarboxylation, are also known to involve oxoiron species 1,3 . Superoxidized iron complexes with (valence) isoelectronic imido and nitrido ligands, as well as 'surface nitrides' , have also been implicated as key intermediates in the nitrogen atom transfer reactions 11 , the biological synthesis of ammonia by the nitrogenase enzyme 12-16 and the industrial Haber-Bosch process 17 .The generation of well-described model compounds can provide vital insights into the mechanism of such enzymatic reactions. Consequently, considerable effort has been made by synthetic chemists to prepare viable models for the putative reaction intermediates in the catalytic cycles of O 2 and N 2 activating enzymes. In this review, we provide an overview of all high-valent oxoiron and nitridoiron species that have been either identified or proposed as reactive intermediates in biology. Subsequently, we summarize some of the recent advances in bioinorganic chemistry that have led to the identification and isolation of iron complexes in unusually high formal oxidation states, containing iron-oxygen or iron-nitrogen multiple bonds. The spectroscopic characterization and the reactivity studies of these model complexes provide vital insights into the mechanism that nature uses to induce the reductive cleavage of dioxygen or dinitrogen in carrying out a number of important biochemical oxidative transformations. Moreover, the comparative review of the electronic structures of the isoelectronic oxoiron and nitridoiron functionalities reveals that the Fe-N bonds are intrinsically more covalent than the Fe-O bonds.

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Compound I and II Analogs of a Chlorin

Cited by 28 publications

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Preparation and Initial Characterization of the Compound I, II, and III States of Iron Methylchlorin-Reconstituted Horseradish Peroxidase and Myoglobin: Models for Key Intermediates in Iron Chlorin Enzymes

Preparation and Initial Characterization of the Compound I, II, and III States of Iron Methylchlorin-Reconstituted Horseradish Peroxidase and Myoglobin: Models for Key Intermediates in Iron Chlorin Enzymes

High-valent iron in chemical and biological oxidations

The biology and chemistry of high-valent iron–oxo and iron–nitrido complexes

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