ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2012
1-Aminocyclopropane-1-carboxylic acid oxidase: insight into cofactor binding from experimental and theoretical studies.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 47 citations in OpenAlex.
- Ethylene signaling and metabolite reprogramming in salt tolerance of Triticum aestivum.Scientific reports · 2026Article
- A tris(pyrazolyl)-based model for the aminocyclopropane carboxylic acid oxidase and its behavior towards oxidants.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Article
- Measuring plant cysteine oxidase interactions with substrates using intrinsic tryptophan fluorescence.Scientific reports · 2024Article
- Biological formation of ethylene.RSC chemical biology · 2023Review
- Genome scale analysis of 1-aminocyclopropane-1-carboxylate oxidase gene family in G. barbadense and its functions in cotton fiber development.Scientific reports · 2023Article
- The Functions of Chloroplastic Ascorbate in Vascular Plants and Algae.International journal of molecular sciences · 2023Review
- Multigenic regulation in the ethylene biosynthesis pathway during coffee flowering.Physiology and molecular biology of plants : an international journal of functional plant biology · 2022Article
- The Multiple Roles of Ascorbate in the Abiotic Stress Response of Plants: Antioxidant, Cofactor, and Regulator.Frontiers in plant science · 2021Review
- Chemical Modification of 1-Aminocyclopropane Carboxylic Acid (ACC) Oxidase: Cysteine Mutational Analysis, Characterization, and Bioconjugation with a Nitroxide Spin Label.Molecular biotechnology · 2019Article
- 1-Aminocyclopropane-1-Carboxylic Acid Oxidase (ACO): The Enzyme That Makes the Plant Hormone Ethylene.Frontiers in plant science · 2019Review
- Ascorbic acid metabolism and functions: A comparison of plants and mammals.Free radical biology & medicine · 2018Review
- Pyrazinamide and derivatives block ethylene biosynthesis by inhibiting ACC oxidase.Nature communications · 2017Article
- Catalytic strategies of the non-heme iron dependent oxygenases and their roles in plant biology.Current opinion in chemical biology · 2016Review
- Catalytic Mechanisms of Fe(II)- and 2-Oxoglutarate-dependent Oxygenases.The Journal of biological chemistry · 2015Review
- Co-operative intermolecular kinetics of 2-oxoglutarate dependent dioxygenases may be essential for system-level regulation of plant cell physiology.Frontiers in plant science · 2015Article
- 1-Aminocyclopropane-1-carboxylic acid oxidase reaction mechanism and putative post-translational activities of the ACCO protein.AoB PLANTS · 2013Article
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
1-Aminocyclopropane-1-carboxylic acid oxidase (ACCO) is a nonheme Fe(II)-containing enzyme that is related to the 2-oxoglutarate-dependent dioxygenase family. The binding of substrates/cofactors to tomato ACCO was investigated through kinetics, tryptophan fluorescence quenching, and modeling studies. α-Aminophosphonate analogs of the substrate (1-aminocyclopropane-1-carboxylic acid, ACC), 1-aminocyclopropane-1-phosphonic acid (ACP) and (1-amino-1-methyl)ethylphosphonic acid (AMEP), were found to be competitive inhibitors versus both ACC and bicarbonate (HCO(3)(-)) ions. The measured dissociation constants for Fe(II) and ACC clearly indicate that bicarbonate ions improve both Fe(II) and ACC binding, strongly suggesting a stabilization role for this cofactor. A structural model of tomato ACCO was constructed and used for docking experiments, providing a model of possible interactions of ACC, HCO(3)(-), and ascorbate at the active site. In this model, the ACC and bicarbonate binding sites are located close together in the active pocket. HCO(3)(-) is found at hydrogen-bond distance from ACC and interacts (hydrogen bonds or electrostatic interactions) with residues K158, R244, Y162, S246, and R300 of the enzyme. The position of ascorbate is also predicted away from ACC. Individually docked at the active site, the inhibitors ACP and AMEP were found coordinating the metal ion in place of ACC with the phosphonate groups interacting with K158 and R300, thus interlocking with both ACC and bicarbonate binding sites. In conclusion, HCO(3)(-) and ACC together occupy positions similar to the position of 2-oxoglutarate in related enzymes, and through a hydrogen bond HCO(3)(-) likely plays a major role in the stabilization of the substrate in the active pocket.
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