Introduction
Carbonic anhydrases (CAs) are zinc(II) metalloenzymes [1] present in almost all living organisms. In mammals, the enzyme is present in several isoforms and, among the 15 isoforms of human carbonic anhydrases (hCA), the most abundant is the second isoform, which is mostly present in blood [2]. CAs catalyze the interconversion between carbon dioxide and hydrogencarbonate. Furthermore, hCA has esterase activity towards esters of carboxylic, sulfonic and phosphoric acid derivatives [3].
The zinc(II) ion present in the active center of hCAII is coordinated by four ligands, His94 and His96 through the Nε2 atoms, His 119 through Nδ1, and a hydroxide ion or a water molecule, depending on pH [4]. The zinc(II) ion can be replaced by a variety of metal ions, such as paramagnetic cobalt(II), nickel(II) and copper(II). It has been shown that if zinc(II) is substituted with cobalt(II), the enzyme maintains a good fraction of its enzymatic activity [[5], [6], [7]], whereas manganese(II), iron(II), copper(II), and nickel(II) hCAII derivatives are inactive [6]. The coordination geometries of the metal-substituted enzymes are different from that of zinc [5,8,9], except for cobalt(II), which remains essentially tetra-coordinated in its active form [5,[10], [11], [12], [13]].
Paramagnetic carbonic anhydrase derivatives have been studied throughout several decades, and even recently they have being used to solve questions regarding the origin of paramagnetic NMR shifts [14]. In particular, the electronic and magnetic properties of high-spin cobalt(II) make it a powerful UV–vis, NMR and EPR spectroscopic probe in biological systems.
Cobalt(II) has a d7 electronic configuration and, when bound to proteins, it commonly adopts a high-spin configuration, with an electronic spin S=3/2 (see Fig. 1). The low symmetry environment of cobalt(II) in proteins removes the orbital degeneracy, making the excited states relatively close in energy to the ground state. This proximity in energy causes the Orbach electron spin relaxation mechanism to be very efficient so that, depending on the geometry of the metal coordination, the electron spin relaxation times typically ranges between 1 and 10ps [15]. This very fast electron relaxation prevents the acquisition of EPR spectra at room temperature. Only around liquid helium temperature electron relaxation is slowed down enough to allow for the acquisition of EPR spectra. Fast electron relaxation, however, provides a rather inefficient mechanism for paramagnetic nuclear spin relaxation, thus the NMR resonances are not severely broadened. The vicinity of the excited states to the ground state is also responsible for large magnetic susceptibility anisotropies (Δχ) [16], which cause large pseudocontact shifts (PCSs) and paramagnetic residual dipolar couplings (RDCs). PCSs and paramagnetic RDCs are long range structural restraints extensively used for the structural characterization of paramagnetic proteins [[17], [18], [19], [20], [21], [22], [23], [24], [25], [26]]. The information content in terms of molecular and electronic structures of paramagnetic NMR shifts and EPR spectra were deeply investigated by F. Ann Walker [[27], [28], [29], [30]], who provided outstanding contributions especially for the characterization of heme proteins and iron complexes.
The binding of inhibitors can change the coordination enviroment of the metal ion. 2D NMR studies of cobalt(II)-CAs adducts started in the 1980's, with the investigation of the ClO4−, NO3− and NCS− ligands in solution [31,32]; these studies continued with the recent works on the oxalate and furosemide adducts of cobalt(II)-hCAII at different pH values [16], and the solid-state NMR studies of the furosemide and sulpiride adducts [33]. The presence of inhibitors can lead to pseudo-tetrahedral coordination, square-pyramidal coordination, or to an equilibrium between the two. Information on the coordination geometry can be obtained from ligand field d-d transitions studies: inhibitors like SCN−, I−, formate, acetate, oxalate, nitrate and 1,2,3-triazole (εmax<200M−1cm−1) give rise to five-coordinate species; sulfonamides, NCO−, CN−, aniline, imidazole (high pH), and 1,2,4-triazole (εmax>300M−1cm−1) give rise to pseudo-tetrahedral species; and HCO3−, N3−, F−, Cl−, Br−, phosphate, benzoate and imidazole (low pH) (εmax=200–300M−1cm−1) lead to four-to-five coordinate equilibria [7].
Also the shape of the EPR spectrum (leading to type A, B, or C classification) has been related to the cobalt coordination number [34]: type A spectra (obtained by binding of acetate, nitrate, thiocyanate, azide or iodide) have two transitions with g values around 6.1–6.8 and 2.3–2.9 and in some cases a third transition around 1.6–1.8; type B spectra (observed by binding of acetazolamide, sulfonamides, cyanate or cyanide) show a sharp feature in the low-field region of the spectrum with g values around 5.8–6.2, 2.2–2.8, and 1.5–1.8; and type C spectra, with a single quasi symmetrical line centered at g values around 3.8–4.0, arise from an excess of ligands like iodide, thiocyanate and imidazole, that may be able to bind in a secondary site inside the active site pocket, thus further modifying the spectral features [34].
The NMR studies have shown that type A and type B ligands have very different magnetic susceptibility anisotropies (Δχ) [16,31,32]. Type A ligands produce Δχ values that are at least twice in absolute value of those of type B ligands, with correspondingly larger PCSs. So far, there are no NMR studies of type C ligands.
The aim of this work is to investigate the effects caused by thiocyanate binding to cobalt(II)-hCAII depending on its concentration. In fact, thiocyanate generates a type A EPR spectrum when added in stoichiometric amounts to cobalt(II)-CA, and a type C spectrum when added in large excess [34]. The evaluation of the magnetic susceptibility anisotropy of cobalt(II)-hCAII in the presence of increasing amounts of thiocyanate may provide information on the origin of the different EPR spectra. In this study, a double mutant of hCAII (DM-hCAII) [14] was used to avoid the binding of metal ions to a secondary site [35].
Section snippets
Double mutant construct
The wild-type form of hCAII was mutated in two positions, H3N and H4N, to avoid the binding of transition metals in the secondary site [9,14,35]. The hCAII double mutant was cloned following a standard PCR protocol.
Expression and purification of DM-hCAII
The expression and purification of DM-hCAII, based on the published protocol [33], was optimized as indicated. The expression vector, pCAM coding the DM-hCAII, was inserted in competent Escherichia coli BL21 (DE3) using a standard heat shock protocol. The culture was in LB-Agar
EPR of cobalt(II)-DM-hCAII
The EPR spectra of cobalt(II)-DM-hCAII were collected in the absence and presence of sodium thiocyanate in 1:1.3 and 1:1357 protein:ligand ratios (Fig. 2). As previously observed for the bovine isoform [34], the spectra change with increasing concentration of sodium thiocyanate. When thiocyanate is added at the same concentration as the protein, it generated a class A spectrum, with g values around 6.8, 2.8 and 1.6. This is consistent with the presence of a 5-coordinated geometry around the
Discussion
Fig. 7 summarises in a qualitative way the main results obtained using several experimental techniques applied to the free protein, the protein in the presence of stoichiometric amounts of thiocyanate, and the protein in thousand-fold excess of thiocyanate. The results are seemingly contradictory: as judged from the EPR spectra, while the stoichiometric addition of thiocyanate causes modest changes in the spectral features, a dramatic change occurs with large excess of thiocyanate; as judged
Author statement
CL, ALM, CFGCG and ER designed the project; JMS, LC, ALC and MF performed all experiments and compiled the data; all authors interpreted and discussed the data; JMS, GP and CL drafted the paper and all authors continued to write, edit and review the manuscript together. All authors have read and agreed to the published version of the manuscript.
Declaration of Competing Interest
The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
Acknowledgements
This work has been supported by the Fondazione Cassa di Risparmio di Firenze. NMR measurements performed at 1200MHz spectrometer were done with the support and the use of resources of Instruct-ERIC, a landmark ESFRI project, and specifically the CERM/CIRMMP Italy center. This work was supported by Fundação para a Ciência e a Tecnologia (FCT-Portugal) for funding UCIBIO project (UIDP/04378/2020 and UIDB/04378/2020) and Associate Laboratory Institute for Health and Bioeconomy – i4HB Project (
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FAQs
What is the mechanism of carbonic anhydrase reaction? ›
Catalytic Mechanism of Carbonic Anhydrases
All the catalytically active CAs reversibly hydrate carbon dioxide to the bicarbonate ion and a proton. Although this reaction may also occur spontaneously, at physiological pH values it is too slow to meet the metabolic needs of most organisms/cells.
The catalytic mechanism of CA II has been studied in particular detail. It involves an attack of zinc-bound OH- on a CO2 molecule loosely bound in a hydrophobic pocket. The resulting zinc-coordinated HCO3- ion is displaced from the metal ion by H2O.
What is the active site of carbonic anhydrase? ›The active site of most carbonic anhydrases contains a zinc ion. They are therefore classified as metalloenzymes. The enzyme maintains acid-base balance and helps transport carbon dioxide.
What happens in the first step of carbonic anhydrase mechanism? ›The first step, deprotonation of the zinc-bound water molecule, is believed to be the rate-limiting step [7,9,10]. After exit of the proton to solution by Grotthus shuttling, the remaining zinc-bound hydroxide executes nucleophilic attack on a CO2 to form HCO 3 − .
What two processes are required to make carbonic anhydrase? ›The enzyme employs a two-step mechanism: in the first step, there is a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide; in the second step, the active site is regenerated by the ionisation of the zinc-bound water molecule and the removal of a proton from the active site.
What reaction does carbonic anhydrase catalyzes quizlet? ›In systemic tissue fluids, the enzyme carbonic anhydrase catalyzes the reaction CO2 + H2O → H2CO3 (which then can dissociate into H+ and HCO3-).
What is the action of carbonic anhydrase enzyme catalyst in human body? ›carbonic anhydrase, enzyme found in red blood cells, gastric mucosa, pancreatic cells, and renal tubules that catalyzes the interconversion of carbon dioxide (CO2) and carbonic acid (H2CO3). Carbonic anhydrase plays an important role in respiration by influencing CO2 transport in the blood.
What is the main function of the enzyme carbonic anhydrase in the body? ›An enzyme present in red blood cells, carbonic anhydrase, aids in the conversion of carbon dioxide to carbonic acid and bicarbonate ions. When red blood cells reach the lungs, the same enzyme helps to convert the bicarbonate ions back to carbon dioxide, which we breathe out.
What is the mechanism of action of carbonic anhydrase inhibitors? ›Mechanism of Action
Acetazolamide is a carbonic anhydrase inhibitor. That means this drug works to cause an accumulation of carbonic acid by preventing its breakdown. The result is lower blood pH (i.e., more acidic), given the increased carbonic acid, which has a reversible reaction into bicarbonate and a hydrogen ion.
Carbonic anhydrase (CA) is a thoroughly studied enzyme. Its primary role is the rapid interconversion of carbon dioxide and bicarbonate in the cells, where carbon dioxide is produced, and in the lungs, where it is released from the blood. At the same time, it regulates pH homeostasis.
How does carbonic anhydrase affect this reaction? ›
Answer and Explanation: In red blood cells, carbonic anhydrase catalyzes the reaction of carbon dioxide (CO2) being converted into into carbonic acid (HCO3-). In full, this reaction breaks down further into bicarbonate ions (HCO3-) and hydrogen ions (H+).
How does carbonic anhydrase increase the rate of reaction? ›The given reaction is catalysed by the enzyme carbonic anhydrase. By using the enzyme present within the cytoplasm, the reaction speeds dramatically with about 600,000 molecules being formed every second. The enzyme has accelerated the reaction rate by about 10 million times.
What type of reaction is carbonic anhydrase? ›Carbonic anhydrase is the enzyme that catalyzes the reversible reactions of carbon dioxide and water: CO 2 + H 2 O ↔ H + + HCO 3 − .
Which chemical reaction between _____ is catalyzed by the enzyme carbonic anhydrase? ›The carbon dioxide produced by cells of the body enter the red blood cells, where carbonic anhydrase catalyzes the reaction between carbon dioxide and water to form carbonic acid.
What are activators of carbonic anhydrase? ›Carbonic anhydrases activators (CAAs) are compounds able to behave as additional shuttles towards the His residue, transferring the proton and activating CAs even more.
Where is carbonic anhydrase found in high concentration in the blood? ›Carbonic anhydrase is found in the blood, gastric mucosa and the minute quantity of same is in plasma. The carbonic anhydrase enzymes work to catalyze the conversion of carbon dioxide and water to the dissociated ions of carbonic acid. This produces bicarbonate anions which get dissolved in the blood plasma.
What is the role of carbon dioxide carbonic anhydrase and carbonic acid in affecting blood pH? ›In the human body, carbon dioxide combines with water via carbonic anhydrase and forms carbonic acid which dissociates into a hydrogen ion and bicarbonate. This is why a reduced respiratory rate will lead to a decreased pH; the more carbon dioxide is exhaled, the less carbon dioxide present for this reaction.
Which of the following equation shows the role of carbonic anhydrase? ›HCO3^ - + H^ + → H2CO3.
How does carbonic anhydrase transport CO2? ›[2] Most of the carbon dioxide diffusing through the capillaries and ultimately into the red blood cells combines with water via a chemical reaction catalyzed by the enzyme carbonic anhydrase catalyzes, forming carbonic acid. Carbonic acid almost immediately dissociates into a bicarbonate anion (HCO3-) and a proton.
Why carbonic anhydrase is fastest enzyme? ›They do not modify the chemical equilibria in any manner but simply make the attainment of equilibrium faster. Carbonic anhydrase catalyzes reversible reaction between carbon dioxide and water to form carbonic acid. This enzyme is one of the fastest enzyme.
What happens to carbonic anhydrase after the products are released? ›
The body eliminates carbon dioxide in the lungs with each exhale. Carbonic anhydrase converts these products into bicarbonate ions that can be transported through the bloodstream.
What is the mechanism of action for carbonic anhydrase inhibitors for hypokalemia? ›Carbonic anhydrase inhibitors, such as acetazolamide, decrease proximal tubular reabsorption of HCO3− in the kidneys by noncompetitive inhibition of luminal and cellular carbonic anhydrase. Hypokalemia is caused by increased sodium delivery to the distal nephron and its reabsorption there in exchange for potassium.
Where does acetazolamide bind to carbonic anhydrase? ›As already mentioned, acetazolamide binds to the zinc atom at the core of the carbonic anhydrase molecule, as well as one other less zinky site. The result of binding at both sites is the complete inhibition of the carbonic anhydrase enzyme.
What happens when carbonic anhydrase is inhibited? ›By inhibition of the enzyme, CAI medications result in the inhibition of the resorption of bicarbonate by the tubular cells, leading to retention of bicarbonate in the tubular lumen.
Which best describes the action of carbonic anhydrase? ›Which best describes the action of carbonic anhydrase? It converts carbon dioxide and water to carbonic acid which dissociates into bicarbonate and hydrogen ions.
What is the mechanism of action of acetazolamide? ›Acetazolamide is a reversible inhibitor of the carbonic anhydrase enzyme that results in reduction of hydrogen ion secretion at the renal tubule and an increased renal excretion of sodium, potassium, bicarbonate, and water.
What is the mechanism of action of carbonic anhydrase inhibitors in mountain sickness? ›Its mechanism is via inhibition of the carbonic anhydrase enzyme which counteracts the respiratory alkalosis which occurs during ascent to altitude. It facilitates the excretion of bicarbonate in the urine. As a result, acetazolamide hastens acclimatization and helps prevent high altitude disorders.
What is the action of carbonic anhydrase enzyme catalyst in the human body? ›carbonic anhydrase, enzyme found in red blood cells, gastric mucosa, pancreatic cells, and renal tubules that catalyzes the interconversion of carbon dioxide (CO2) and carbonic acid (H2CO3). Carbonic anhydrase plays an important role in respiration by influencing CO2 transport in the blood.
What are the two reactions in the reaction catalyzed by carbonic anhydrase? ›The first reaction—the CO2 hydration/carbonic acid (H2CO3) dehydration reaction—is very slow. The second reaction—the dissociation or ionization of H2CO3—is extremely rapid and is always at equilibrium under physiological conditions [55].
Which reaction does carbonic anhydrase catalyze quizlet? ›In systemic tissue fluids, the enzyme carbonic anhydrase catalyzes the reaction CO2 + H2O → H2CO3 (which then can dissociate into H+ and HCO3-).
What ions are formed when carbonic anhydrase catalyzes the reaction? ›
Answer and Explanation: In red blood cells, carbonic anhydrase catalyzes the reaction of carbon dioxide (CO2) being converted into into carbonic acid (HCO3-). In full, this reaction breaks down further into bicarbonate ions (HCO3-) and hydrogen ions (H+).
What is the main function of acetazolamide? ›Acetazolamide is used to treat glaucoma, a condition in which increased pressure in the eye can lead to gradual loss of vision. Acetazolamide decreases the pressure in the eye.
What is the synthesis reaction of acetazolamide? ›The synthesis of acetazolamide is based on the production of 2-amino-5-mercapto-1,3, 4-thiadiazole (9.7. 2), which is synthesized by the reaction of ammonium thiocyanate and hydrazine, forming hydrazino-N,N′-bis-(thiourea) (9.7. 1), which cycles into thiazole (9.7.
How does acetazolamide stimulate respiration? ›Acetazolamide is used as a respiratory stimulant in subjects with COPD [30]. The classic explanation of why acetazolamide acts as a respiratory stimulant is through the inhibition of the renal CA enzyme, which in turn induces a decrease of serum bicarbonate and serum pH.
Which of the following is a side effect of a carbonic anhydrase inhibitor? ›Potential side effects of oral CAIs include metabolic acidosis and hypokalemia, manifested as panting, depression, vomiting, diarrhea, and collapse. If any of these side effects are noted, discontinue CAI therapy. Symptoms should resolve within 24 hours, and therapy can be reinstituted at a decreased dosage.
What is the role of carbonic anhydrase How does it facilitate the transport of CO2? ›[2] Most of the carbon dioxide diffusing through the capillaries and ultimately into the red blood cells combines with water via a chemical reaction catalyzed by the enzyme carbonic anhydrase catalyzes, forming carbonic acid. Carbonic acid almost immediately dissociates into a bicarbonate anion (HCO3-) and a proton.
What is the function of the enzyme carbonic anhydrase and where is it found in the body? ›An enzyme present in red blood cells, carbonic anhydrase, aids in the conversion of carbon dioxide to carbonic acid and bicarbonate ions. When red blood cells reach the lungs, the same enzyme helps to convert the bicarbonate ions back to carbon dioxide, which we breathe out.
Where is high concentration of carbonic anhydrase present in the body? ›Carbonic anhydrase is found in the blood, gastric mucosa and the minute quantity of same is in plasma. The carbonic anhydrase enzymes work to catalyze the conversion of carbon dioxide and water to the dissociated ions of carbonic acid. This produces bicarbonate anions which get dissolved in the blood plasma.