PubMed · 6653950
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1983. Orphan biologic licensed.. https://pubmed.ncbi.nlm.nih.gov/6653950/
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Heme, an organometallic tetrapyrrole, is widely engaged in oxygen transport, electron delivery, enzymatic reactions, and signal transduction. In plants, it is also involved in photomorphogenesis and photosynthesis. HEME OXYGENASE 1 (HO1) initiates the first committed step in heme catabolism, and it has generally been thought that this reaction takes place in chloroplasts. Here, we show that HO1 in both Arabidopsis (Arabidopsis thaliana) and rice (Oryza sativa) has 2 transcription start sites (TSSs), producing long (HO1L) and short (HO1S) transcripts. Their products localize to the chloroplast and the cytosol, respectively. During early development or de-etiolation, the HO1L/HO1S ratio gradually increases. Light perception via phytochromes (Phys) and cryptochromes elevates the HO1L/HO1S ratio in the whole seedling through the functions of ELONGATED HYPOCOTYL 5 (HY5) and HY5 HOMOLOG and through the suppression of DE-ETIOLATED 1, CONSTITUTIVE PHOTOMORPHOGENESIS 1, and PHYTOCHROME INTERACTING FACTORs. HO1L introduction complements the HO1-deficient mutant; surprisingly, HO1S expression also restores the short hypocotyl phenotype and high pigment content and helps the mutant recover from the genomes uncoupled (gun) phenotype. This indicates the assembly of functional Phys within these lines. Furthermore, our findings support the hypothesis that a mobile heme signal is involved in retrograde signaling from the chloroplast. Altogether, our work clarifies the molecular mechanism of HO1 TSS regulation and highlights the presence of a cytosolic bypass for heme catabolism in plant cells.
An iron-containing, tetrapyrrole ring, heme is an essential prosthetic group in an array of proteins that comprehensively affect cellular function and metabolism; yet "free" heme in sufficient amounts can be damaging to the kidney and other organs because of its bioreactivity and pro-oxidant effects. This review discusses the cellular metabolism of heme in health and disease and covers such areas as the synthesis of heme and its utilization in heme proteins; mechanisms underlying the toxicity of heme; and the extent to which pathophysiologic processes, such as renal incorporation of heme proteins or destabilization of intracellular heme proteins, increase intracellular levels of heme and provoke renal injury. The main catabolic process that degrades heme, the heme oxygenase (HO) system, is reviewed, and evidence for the protective effects of HO-1 against acute and chronic heme/heme protein-induced renal injury is summarized. Finally, current views regarding the molecular basis for heme-induced upregulation of HO-1 are discussed.
Nonheme and heme iron monooxygenases participate in oxidative N-dealkylation reactions in nature, and high-valent oxoiron(IV) species have been invoked as active oxidants that effect the oxygenation of organic substrates. The present study describes the first example of the oxidative N-dealkylation of N,N-dialkylamines by synthetic nonheme oxoiron(IV) complexes and the reactivity comparisons of nonheme and heme oxoiron(IV) complexes. Detailed mechanistic studies were performed with various N,N-dialkylaniline substrates such as para-substituted N,N-dimethylanilines, para-chloro-N-ethyl-N-methylaniline, para-chloro-N-cyclopropyl-N-isopropylaniline, and deuteriated N,N-dimethylanilines. The results of a linear free-energy correlation, inter- and intramolecular kinetic isotope effects, and product analysis studied with the mechanistic probes demonstrate that the oxidative N-dealkylation reactions by nonheme and heme oxoiron(IV) complexes occur via an electron transfer-proton transfer (ET-PT) mechanism.